Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-38313	Ser1026	PQQGFFSsPSTSRTP	Homo sapiens	A-431 Cell
pmid	sentence
8360196	Using a synthetic peptide corresponding to the sequence surrounding ser-1002, p34cdc2 was identified as a kinase capable of phosphorylating this serine residue. phosphorylation of the egf receptor by p34cdc2 was associated with a decrease in its tyrosine protein kinase activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273638	Ser105	KFGLTFQsPADARAF	Homo sapiens	HEK-293 Cell
pmid	sentence
32697994	We show that oncogenic EGFR(L858R) signaling leads to the phosphorylation of SPRED1 on serine 105, disrupting the SPRED1-neurofibromin complex. The structural, biochemical, and biological results provide new mechanistic insights about how SPRED1 interacts with neurofibromin and regulates active KRAS levels in normal and pathologic conditions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250619	Ser1064	SCPIKEDsFLQRYSS	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250620	Ser1070	DSFLQRYsSDPTGAL	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250621	Ser1071	SFLQRYSsDPTGALT	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250622	Ser1081	TGALTEDsIDDTFLP	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250623	Ser1120	QPLNPAPsRDPHYQD	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250624	Ser1166	QKGSHQIsLDNPDYQ	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250625	Ser768	DEAYVMAsVDNPHVC	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Publications:

7

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Cell Line
SIGNOR-250694	Ser1070	DSFLQRYsSDPTGAL	A-431 Cell
pmid	sentence
1309762	The mechanism of desensitization of kinase activity can be accounted for, in part, by the EGF-stimulated phosphorylation of the receptor at Ser1046/7, a substrate for the multifunctional calmodulin-dependent protein kinase II in vitro. Mutation of Ser1046/7 by replacement with Ala residues blocks desensitization of the EGF receptor protein-tyrosine kinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250695	Ser1071	SFLQRYSsDPTGALT	Homo sapiens	A-431 Cell
pmid	sentence
1309762	The mechanism of desensitization of kinase activity can be accounted for, in part, by the EGF-stimulated phosphorylation of the receptor at Ser1046/7, a substrate for the multifunctional calmodulin-dependent protein kinase II in vitro. Mutation of Ser1046/7 by replacement with Ala residues blocks desensitization of the EGF receptor protein-tyrosine kinase activity.

Publications:

2

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264419	Ser2054	GGNKRKLsTAMALIG	Homo sapiens	HeLa Cell
pmid	sentence
12196520	We further provide in vitro evidence that epidermal growth factor receptor (EGFR)-mediated phosphorylation regulated ABCA1 ubiquitination \|The EGFR selective inhibitor PD168393 blocked the EGFR-ABCA1 interaction and abolished ABCA1Ser2054 phosphorylation\|

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277589	Thr430	LEIIRGRtKQHGQFS	in vitro
pmid	sentence
35226996	Recombinant PKG II inhibited the epidermal growth factor (EGF)-induced activation of the EGF receptor via phosphorylating the T406 of the extracellular domain and blocked EGF-triggered proliferation of various cancer cells.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248858	Thr678	RHIVRKRtLRRLLQE	Mus musculus
pmid	sentence
1860884	These data indicate that activation of protein kinase C and subsequent phosphorylation of the EGF receptor at T654 lead to rapid physiological attenuation of EGF receptor signaling.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-174755	Thr678	RHIVRKRtLRRLLQE	Homo sapiens
pmid	sentence
21749319	This identified thr654 in egfr as the pkn1 phosphorylation siteit has been shown that the phosphorylation of egfr at thr654 by pkc reduces the tyrosine kinase activity of the receptor

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-77421	Thr678	RHIVRKRtLRRLLQE	Homo sapiens
pmid	sentence
10816576	Biochemical and morphological analyses indicate that threonine-phosphorylated EGFR molecules undergo normal internalization, but instead of sorting to lysosomal degradation, they recycle back to the cell surfaceThe inhibitory effects of pkc are mediated by a single threonine residue (threonine 654) of egfr

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-20545	Thr693	RELVEPLtPSGEAPN	in vitro
pmid	sentence
1651322	A growth factor-stimulated protein kinase activity that phosphorylates the epidermal growth factor (EGF) receptor at Thr669 has been described Anion-exchange chromatography demonstrated that this protein kinase activity was accounted for by two enzymes. The first peak of activity eluted from the column corresponded to the microtubule-associated protein 2 (MAP2) kinase

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-244529	Thr693	RELVEPLtPSGEAPN	Homo sapiens
pmid	sentence
10816576	It is likely that the map2 and ert kinases account for the phosphorylation of the egf receptor at thr669 (egf receptor (krel veplt669psgeapnqallr)) observed in cultured cells.Phosphorylation at ser-695 is partial and occurs only if thr-693 is phosphorylated. Phosphorylation at thr-678 and thr-693 by prkd1 inhibits egf-induced mapk8/jnk1 activation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, EGFR Signaling, FLT3-ITD in AML, Glioblastoma Multiforme, Hepatocellular Tumor, Noonan syndrome, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, SARS-CoV MAPK PERTURBATION

Identifier	Residue	Sequence	Organism
SIGNOR-20549	Thr693	RELVEPLtPSGEAPN	Homo sapiens
pmid	sentence
1651322	It is likely that the map2 and ert kinases account for the phosphorylation of the egf receptor at thr669 (egf receptor (krel veplt669psgeapnqallr)) observed in cultured cells.Phosphorylation at ser-695 is partial and occurs only if thr-693 is phosphorylated. Phosphorylation at thr-678 and thr-693 by prkd1 inhibits egf-induced mapk8/jnk1 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266335	Tyr100	FDKDGNGyISAAELR	Homo sapiens
pmid	sentence
3415247	Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-24778	Tyr100	FDKDGNGyISAAELR	Homo sapiens
pmid	sentence
3415247	Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule.

Identifier	Residue	Sequence	Organism
SIGNOR-34691	Tyr100	FDKDGNGyISAAELR	Homo sapiens
pmid	sentence
7925415	Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266319	Tyr100	FDKDGNGyISAAELR	Homo sapiens
pmid	sentence
3415247	Phosphorylation of calmodulin by the epidermal-growth-factor-receptor tyrosine kinase. Phosphorylated calmodulin does not exhibit the characteristic ca2+ shift normally observed with calmodulin in electrophoretic gels, an observation that is consistent with this modification affecting the biological activity of the molecule.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236475	Tyr1016	DVVDADEyLIPQQGF	Homo sapiens	HeLa Cell
pmid	sentence
10653583	After binding of epidermal growth factor (EGF), the EGF receptor (EGFR) becomes autophosphorylated via tyrosine.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236527	Tyr1016	DVVDADEyLIPQQGF	Mus musculus	32D Cell
pmid	sentence
16122376	EGFR possesses three major and two minor tyrosine autophosphorylation sites located at Y1068, Y1148, Y1173, and at Y992 and Y1086 respectively. In addition, EGFR Y1114 is preceded by glutamic acid (Figure 1), which should be preferred by the EGFR kinase as indicated in previous work

Identifier	Residue	Sequence	Organism
SIGNOR-251093	Tyr1069	EDSFLQRySSDPTGA	Homo sapiens
pmid	sentence
10635327	Initially, an autophosphorylation reaction creates docking sites for several signaling proteins, including a Cbl binding site at tyrosine 1045 of EGFR.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236479	Tyr1092	TFLPVPEyINQSVPK	Homo sapiens	HeLa Cell
pmid	sentence
10653583	After binding of epidermal growth factor (EGF), the EGF receptor (EGFR) becomes autophosphorylated via tyrosine.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236523	Tyr1092	TFLPVPEyINQSVPK	Mus musculus	32D Cell
pmid	sentence
16122376	EGFR possesses three major and two minor tyrosine autophosphorylation sites located at Y1068, Y1148, Y1173, and at Y992 and Y1086 respectively. In addition, EGFR Y1114 is preceded by glutamic acid (Figure 1), which should be preferred by the EGFR kinase as indicated in previous work

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236516	Tyr1110	GSVQNPVyHNQPLNP	Mus musculus	32D Cell
pmid	sentence
16122376	EGFR possesses three major and two minor tyrosine autophosphorylation sites located at Y1068, Y1148, Y1173, and at Y992 and Y1086 respectively. In addition, EGFR Y1114 is preceded by glutamic acid (Figure 1), which should be preferred by the EGFR kinase as indicated in previous work

Identifier	Residue	Sequence	Organism
SIGNOR-236483	Tyr1110	GSVQNPVyHNQPLNP	Homo sapiens
pmid	sentence
10653583	After binding of epidermal growth factor (EGF), the EGF receptor (EGFR) becomes autophosphorylated via tyrosine.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236531	Tyr1172	ISLDNPDyQQDFFPK	Mus musculus	32D Cell
pmid	sentence
16122376	EGFR possesses three major and two minor tyrosine autophosphorylation sites located at Y1068, Y1148, Y1173, and at Y992 and Y1086 respectively. In addition, EGFR Y1114 is preceded by glutamic acid (Figure 1), which should be preferred by the EGFR kinase as indicated in previous work

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236467	Tyr1172	ISLDNPDyQQDFFPK	Homo sapiens	HeLa Cell
pmid	sentence
10653583	After binding of epidermal growth factor (EGF), the EGF receptor (EGFR) becomes autophosphorylated via tyrosine.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235951	Tyr1197	STAENAEyLRVAPQS	Mus musculus	32D Cell
pmid	sentence
16122376	EGFR possesses three major and two minor tyrosine autophosphorylation sites located at Y1068, Y1148, Y1173, and at Y992 and Y1086 respectively. In addition, EGFR Y1114 is preceded by glutamic acid (Figure 1), which should be preferred by the EGFR kinase as indicated in previous work

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236471	Tyr1197	STAENAEyLRVAPQS	Homo sapiens	HeLa Cell
pmid	sentence
10653583	After binding of epidermal growth factor (EGF), the EGF receptor (EGFR) becomes autophosphorylated via tyrosine.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236487	Tyr869	LGAEEKEyHAEGGKV	Homo sapiens	HeLa Cell
pmid	sentence
10653583	After binding of epidermal growth factor (EGF), the EGF receptor (EGFR) becomes autophosphorylated via tyrosine.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235956	Tyr869	LGAEEKEyHAEGGKV	Mus musculus	32D Cell
pmid	sentence
16122376	EGFR possesses three major and two minor tyrosine autophosphorylation sites located at Y1068, Y1148, Y1173, and at Y992 and Y1086 respectively. In addition, EGFR Y1114 is preceded by glutamic acid (Figure 1), which should be preferred by the EGFR kinase as indicated in previous work

Publications:

13

Organism:

Homo Sapiens, Mus Musculus

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, EGFR Signaling, FLT3-ITD in AML, Glioblastoma Multiforme, Hepatocellular Tumor, Noonan syndrome, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, SARS-CoV MAPK PERTURBATION

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248532	Tyr1016	DVVDADEyLIPQQGF	Homo sapiens	NCI-H1299 Cell
pmid	sentence
21262974	We found that EGF receptor (EGFR) was a direct substrate of VHR and that overexpression of VHR down-regulated EGFR phosphorylation, particularly at Tyr-992 residue. Expression of VHR inhibited the activation of phospholipase Cγ and protein kinase C, both downstream effectors of Tyr-992 phosphorylation of EGFR.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-44239	Tyr1016	DVVDADEyLIPQQGF	Homo sapiens
pmid	sentence
8845374	The c-terminal autophosphorylation domain of egfr was extensively phosphorylated by c-src./These studies revealed that y1086 was phosphorylated to a significantly higher extent by c-src than by egfr. Additionally, y1101 was identified as a unique c-src phosphorylation site

Identifier	Residue	Sequence	Organism
SIGNOR-44243	Tyr1110	GSVQNPVyHNQPLNP	Homo sapiens
pmid	sentence
8845374	The c-terminal autophosphorylation domain of egfr was extensively phosphorylated by c-src./These studies revealed that y1086 was phosphorylated to a significantly higher extent by c-src than by egfr. Additionally, y1101 was identified as a unique c-src phosphorylation site.

Identifier	Residue	Sequence	Organism
SIGNOR-44251	Tyr1172	ISLDNPDyQQDFFPK	Homo sapiens
pmid	sentence
8845374	Revealed that peptides derived from egfr residues y992, y1086, y1101, and y1148 bound directly to the sh2 domain of c-src (figure 8c). These experiments demonstrate that a specific subset of egfr receptor c-src phosphorylation sites are also ligands for the sh2 domain of c-src.Cellular src functions as a co-transducer of transmembrane signals emanating from a variety of growth factor receptors, including egfr

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235921	Tyr869	LGAEEKEyHAEGGKV	Homo sapiens	Fibroblast
pmid	sentence
11983694	In summary, this study describes a novel mechanism for metal-induced egfr transactivation, which is likely to be mediated by src through the phosphorylation site of tyr-845 on egfr. emanating from a variety of growth factor receptors, including egfry845 (e-e-k-e-y845-h-a-e)

Publications:

4

Organism:

Homo Sapiens

Pathways:

EGFR Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236424	Tyr1016	DVVDADEyLIPQQGF	Chlorocebus aethiops	COS Cell
pmid	sentence
12582165	Given that substrate trapping occurred in intact cells and that the interaction was very specific, it is highly likely that egfr and gab1 represent physiological shp2 substrates.To further confirm that phosphotyrosyl proteins trapped by SHP2 are target substrates, we carried out an immunocomplex in vitrophosphatase assay.The WT protein partially dephosphorylated both the EGFR and Gab1, whereas the DM protein did not

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248666	Tyr1016	DVVDADEyLIPQQGF	Chlorocebus aethiops	COS Cell
pmid	sentence
14560030	Inhibition is achieved through the dephosphorylation of RasGAP binding sites at the level of the plasma membrane. We have identified Tyr992 of the epidermal growth factor receptor (EGFR) to be one such site, since its mutation to Phe renders the EGFR refractory to the effect of dominant-negative SHP2. To our knowledge, this is the first report to outline the site and molecular mechanism of action of SHP2 in EGFR signaling,

Publications:

2

Organism:

Chlorocebus Aethiops

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, Noonan syndrome

Identifier	Residue	Sequence	Organism
SIGNOR-248407	Tyr1016	DVVDADEyLIPQQGF	in vitro
pmid	sentence
8621392	We have shown previously that amino acid residues flanking the phosphotyrosine are important for efficient PTP1 catalysis (Table 1 and Refs. 9, 10, and 17). For example, the kcat/Km value for the undecapeptide, EGFR988-989 (epidermal growth factor autophosphorylation site Tyr992, residues 988-998) (Asp-Ala-Asp-Glu-pTyr-Leu-Ile-Pro-Gln-Gln-Gly) is 3220-fold higher than that of phosphotyrosine (Table 1). We further demonstrated that a minimum of six amino acid residues are required for the most efficient PTP1 binding and catalysis.

Identifier	Residue	Organism
SIGNOR-276981		Homo sapiens
pmid	sentence
18253097	The protein tyrosine phosphatase, PTP1B, is known to negatively regulate EGF-induced signaling in several cell types by dephosphorylating the epidermal growth factor receptor (EGFR).\|Together, these findings provide evidence that PTP1B plays a role in the negative regulation of EGFR signaling in rat corneal endothelial cells, at least at the level of Tyr992 phosphorylation.

Publications:

2

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277190	Tyr102	YDLKLQEyQSAIKVE	Homo sapiens
pmid	sentence
26718225	Here, we found that nuclear EGFR induced phosphorylation of PPARγ at Tyr-74 leading to PPARγ ubiquitination and degradation by mouse double minute 2 (MDM2) ubiquitin ligase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248697	Tyr1069	EDSFLQRySSDPTGA	Homo sapiens	HeLa Cell
pmid	sentence
19836242	We report the identification of PTPRK and PTPRJ (density-enhanced phosphatase-1 [DEP-1]) as EGFR-targeting phosphatases. DEP-1 is a tumor suppressor that dephosphorylates and thereby stabilizes EGFR by hampering its ability to associate with the CBL-GRB2 ubiquitin ligase complex\|By employing commercially available antibodies, which are supposed to recognize specific tyrosine phosphorylation sites of EGFR, we found that depletion of endogenous DEP-1 nonselectively increased receptor phosphorylation, affecting all three sites we analyzed (tyrosines 1045, 1068, and 1173

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248698	Tyr1092	TFLPVPEyINQSVPK	Homo sapiens	HeLa Cell
pmid	sentence
19836242	We report the identification of PTPRK and PTPRJ (density-enhanced phosphatase-1 [DEP-1]) as EGFR-targeting phosphatases. DEP-1 is a tumor suppressor that dephosphorylates and thereby stabilizes EGFR by hampering its ability to associate with the CBL-GRB2 ubiquitin ligase complex\|By employing commercially available antibodies, which are supposed to recognize specific tyrosine phosphorylation sites of EGFR, we found that depletion of endogenous DEP-1 nonselectively increased receptor phosphorylation, affecting all three sites we analyzed (tyrosines 1045, 1068, and 1173

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248699	Tyr1197	STAENAEyLRVAPQS	Homo sapiens	HeLa Cell
pmid	sentence
19836242	We report the identification of PTPRK and PTPRJ (density-enhanced phosphatase-1 [DEP-1]) as EGFR-targeting phosphatases. DEP-1 is a tumor suppressor that dephosphorylates and thereby stabilizes EGFR by hampering its ability to associate with the CBL-GRB2 ubiquitin ligase complex\|By employing commercially available antibodies, which are supposed to recognize specific tyrosine phosphorylation sites of EGFR, we found that depletion of endogenous DEP-1 nonselectively increased receptor phosphorylation, affecting all three sites we analyzed (tyrosines 1045, 1068, and 1173

Publications:

3

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML

Identifier	Residue	Sequence	Organism
SIGNOR-251347	Tyr1069	EDSFLQRySSDPTGA	Chlorocebus aethiops
pmid	sentence
9363897	Tyrosine at residue 1,068 of the EGFR is proposed to be one of the principal phosphorylation sites and Grb2-binding sites stimulated by growth hormone via Jak2. Our results indicate that the role of EGFR in signalling by growth hormone is to be phosphorylated by Jak2, thereby providing docking sites for Grb2 and activating MAP kinases and gene expression, independently of the intrinsic tyrosine kinase activity of EGFR.¬†

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

Acute Myeloid Leukemia, EGFR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-254699	Tyr1069	EDSFLQRySSDPTGA	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276490	Tyr109	KRKRLSDyALIFGMF	Homo sapiens	HEK-293 Cell
pmid	sentence
23496660	These results demonstrate the novel information that hSKCa1 channels are inhibited by genistein, T25 and AG556 via EGFR tyrosine kinase inhibition, which is related to the phosphorylation of Tyr(109) in the N-terminus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248722	Tyr1092	TFLPVPEyINQSVPK	Cricetulus griseus	CHO Cell
pmid	sentence
16263724	RPTP-kappa also reduced epidermal growth factor-dependent EGFR tyrosine phosphorylation in CHO cells. Purified RPTP-kappa preferentially dephosphorylated EGFR tyrosines 1068 and 1173 in vitro.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248723	Tyr1197	STAENAEyLRVAPQS	Cricetulus griseus	CHO Cell
pmid	sentence
16263724	RPTP-kappa also reduced epidermal growth factor-dependent EGFR tyrosine phosphorylation in CHO cells. Purified RPTP-kappa preferentially dephosphorylated EGFR tyrosines 1068 and 1173 in vitro.

Publications:

2

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism
SIGNOR-44247	Tyr1125	APSRDPHyQDPHSTA	Homo sapiens
pmid	sentence
8845374	The c-terminal autophosphorylation domain of egfr was extensively phosphorylated by c-src./These studies revealed that y1086 was phosphorylated to a significantly higher extent by c-src than by egfr. Additionally, y1101 was identified as a unique c-src phosphorylation site

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-254700	Tyr1172	ISLDNPDyQQDFFPK	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

Identifier	Residue	Sequence	Organism
SIGNOR-149273	Tyr1172	ISLDNPDyQQDFFPK	Homo sapiens
pmid	sentence
16943190	We show that activated abl phosphorylates the egfr primarily on tyrosine 1173.

Identifier	Residue	Sequence	Organism
SIGNOR-149277	Tyr1197	STAENAEyLRVAPQS	Homo sapiens
pmid	sentence
16943190	we show that activated Abl phosphorylates the EGFR primarily on tyrosine 1173Furthermore, we show that activated Abl allows the ligand-activated EGFR to escape Cbl-dependent down-regulation by inhibiting the accumulation of Cbl at the plasma membrane in response to epidermal growth factor stimulation and disrupting the formation of the EGFR.Cbl complex without affecting Cbl protein stability. These findings reveal a novel role for Abl in promoting increased cell-surface expression of the EGFR and suggest that Abl/EGFR signaling may cooperate in human

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-59965	Tyr1197	STAENAEyLRVAPQS	Homo sapiens
pmid	sentence
9733788	The sh2-domain ptpase shp-1 binds to and dephosphorylates autophosphorylated egfr and may participate in modulation of egfr signaling in epithelial cells. Reduced shp-1 binding to the egfr y1173f mutant resulted in a reduced receptor dephosphorylation by coexpressed shp-1 and less interference with egf-dependent mitogen-activated protein kinase stimulation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-109538	Tyr1229	SSTDRSPyEKVSAGN	Homo sapiens	Breast Cancer Cell
pmid	sentence
11483589	We also show that the activated egf-r phosphorylates the muc1 cytoplasmic tail on tyrosine at a yekv motif that functions as a binding site for the c-src sh2 domain. The results demonstrate that egf-r-mediated phosphorylation of muc1 induces binding of muc1 to c-src in cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251094	Tyr1248	PTAENPEyLGLDVPV	Homo sapiens	Breast Cancer Cell Line
pmid	sentence
12354693	Induction of cancer cell migration by epidermal growth factor is initiated by specific phosphorylation of tyrosine 1248 of c-erbB-2 receptor via EGFR. \| In summary, c-erbB-2 up-regulation switches on the cell migration program by modulating the time course of PLC-gamma1 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-20976	Tyr1253	EGSFESRyQQPFEDF	Homo sapiens
pmid	sentence
1689310	We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation.

Identifier	Residue	Sequence	Organism
SIGNOR-20980	Tyr472	KLAEGSAyEEVPTSM	Homo sapiens
pmid	sentence
1689310	We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation.

Identifier	Residue	Sequence	Organism
SIGNOR-20984	Tyr771	IGTAEPDyGALYEGR	Homo sapiens
pmid	sentence
1689310	We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation.

Identifier	Residue	Sequence	Organism
SIGNOR-48872	Tyr783	EGRNPGFyVEANPMP	Homo sapiens
pmid	sentence
9176240	In contrast, egf-induced tyrosine phosphorylation of plc-gamma 1 was rather small, indicating that tyrosine phosphorylation of plc-gamma 1 is not proportional to changes in plc activity. These results suggest that autophosphorylation of theegfr may induce a conformational change of its kinase domain which enhances its kinase activity with exogenous substrates and may induce association with phospholipase c-gamma by increasing its affinity to a domain containing tyr-771.

Publications:

4

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-34748	Tyr1276	GGGPGGDyAAMGACP	Homo sapiens	Breast Cancer Cell
pmid	sentence
7929151	The erbb3 protein which possesses little or no intrinsic protein tyrosine kinase activiity is phosphorylated by the activated egf receptor protein tyrosine kinase on tyrosine residues within the yxxm sequence motif. These phosphorylated tyrosine residues interact with the p85 regulatory subunit of pi 3-kinase, which could result in the activation of the p110 catalytic subunit via a conformational mechanism.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-34752	Tyr1289	CPASEQGyEEMRAFQ	Homo sapiens	Breast Cancer Cell
pmid	sentence
7929151	The erbb3 protein which possesses little or no intrinsic protein tyrosine kinase activiity is phosphorylated by the activated egf receptor protein tyrosine kinase on tyrosine residues within the yxxm sequence motif. These phosphorylated tyrosine residues interact with the p85 regulatory subunit of pi 3-kinase, which could result in the activation of the p110 catalytic subunit via a conformational mechanism.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275549	Tyr136	GDCCYEEyKDRKREN
pmid	sentence
22198508	Our results demonstrate that human atrial I(to) and cloned hKv4.3 channels are modulated by EGFR kinase via phosphorylation of the Y136 residue and by Src-family kinases via phosphorylation of the Y108 residue\|We found that human atrial I(to) was inhibited by the broad-spectrum PTK inhibitor genistein, the selective epidermal growth factor receptor (EGFR) kinase inhibitor AG556, and the Src-family kinases inhibitor PP2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276397	Tyr136	GDCCYEEyKDRKREN	Homo sapiens	HEK-293 Cell
pmid	sentence
22198508	These results indicate that Y108 (for Src-family kinases) and Y136 (for EGFR kinase) are involved in the tyrosine phosphorylation of hKv4.3 channels.

Publications:

2

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-95972	Tyr142	TENDDDVyRSLEELA	Homo sapiens
pmid	sentence
12454019	To understand the mechanism of egf-dependent vav2 activation, we examined first the egf-dependent phosphorylation sites on vav2 and the nature of interaction of vav2 with the activated egf receptor. Based on our in vitro and in vivo data all three tyrosine residues (142, 159, and 172) in the n-terminal domain of vav2 can be phosphorylated by the egf receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-95976	Tyr159	HDLGEDIyDCVPCED	Homo sapiens
pmid	sentence
12454019	To understand the mechanism of egf-dependent vav2 activation, we examined first the egf-dependent phosphorylation sites on vav2 and the nature of interaction of vav2 with the activated egf receptor. Based on our in vitro and in vivo data all three tyrosine residues (142, 159, and 172) in the n-terminal domain of vav2 can be phosphorylated by the egf receptor.

Identifier	Residue	Sequence	Organism
SIGNOR-95980	Tyr172	EDGGDDIyEDIIKVE	Homo sapiens
pmid	sentence
12454019	To understand the mechanism of egf-dependent vav2 activation, we examined first the egf-dependent phosphorylation sites on vav2 and the nature of interaction of vav2 with the activated egf receptor. Based on our in vitro and in vivo data all three tyrosine residues (142, 159, and 172) in the n-terminal domain of vav2 can be phosphorylated by the egf receptor.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-133219	Tyr146	KEVHKSGyLSSERLI	Homo sapiens	A-431 Cell
pmid	sentence
15647376	Here we report the identification of the tyrosine phosphorylation sites in ezrin using bacterially expressed protein as a substrate for in vitro phosphorylation with the egf receptor. tyrosines 145 and 353 were identified as the sites of phosphorylation. but as of yet the role of ezrin phosphorylation at y145 is unknown.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277197	Tyr148	KITLDNAyMEKCDEN	Homo sapiens	MDA-MB-468 Cell
pmid	sentence
26759242	EGFR binds to and phosphorylates PKM2 to inhibit its activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277242	Tyr153	GEEGQSIyKLTDFGA	Homo sapiens
pmid	sentence
27287717	EGFRL858R/T790M phosphorylates IKBKE at tyrosine residues. While wild-type and mutant EGFR directly interacted with IKBKE, only mutant EGFR phosphorylated IKBKE on residues Y153 and Y179.

Identifier	Residue	Sequence	Organism
SIGNOR-277243	Tyr179	SVYGTEEyLHPDMYE	Homo sapiens
pmid	sentence
27287717	EGFRL858R/T790M phosphorylates IKBKE at tyrosine residues. While wild-type and mutant EGFR directly interacted with IKBKE, only mutant EGFR phosphorylated IKBKE on residues Y153 and Y179.

Publications:

2

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism
SIGNOR-277227	Tyr154	QLNDSAAyYLNDLDR	in vitro
pmid	sentence
33139573	RTKs directly phosphorylate Gαi on Y154, 155, and Y320.

Identifier	Residue	Sequence	Organism
SIGNOR-277226	Tyr155	LNDSAAYyLNDLDRI	in vitro
pmid	sentence
33139573	RTKs directly phosphorylate Gαi on Y154, 155, and Y320.

Identifier	Residue	Sequence	Organism
SIGNOR-277228	Tyr320	RKDTKEIyTHFTCAT	in vitro
pmid	sentence
33139573	RTKs directly phosphorylate Gαi on Y154, 155, and Y320.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-98267	Tyr168	TLMEKDSyPRFLKSP	Homo sapiens
pmid	sentence
12588871	Phosphorylation on tyr(168) was mediated by the epidermal growth factor receptor (egfr). We show here that endogenous rgs16 is phosphorylated after epidermal growth factor stimulation of mcf-7 cells.

Identifier	Residue	Sequence	Organism
SIGNOR-111024	Tyr177	RFLKSPAyRDLAAQA	Homo sapiens
pmid	sentence
11602604	Rgs16 contains two conserved tyrosine residues in the rgs box, tyr(168) and tyr(177), which are predicted sites of phosphorylation. Rgs16 underwent phosphorylation in response to m2 muscarinic receptor or egfr stimulation in hek 293t or cos-7 cells, which required egfr kinase activity. Mutational analysis suggested that rgs16 was phosphorylated on both tyrosine residues (tyr(168) tyr(177)) after egf stimulation.Phosphorylated rgs16 demonstrated enhanced gtpase accelerating (gap) activity on galpha(i). Mutation of tyr(168) to phenylalanine resulted in a 30% diminution in rgs16 gap activity mutation of tyr(177) to phenylalanine had no effect on rgs16 gap activity but also abolished its regulation of g(i)-mediated signal transduction in these cells.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251095	Tyr179	RLLTMSFyRNYHAMT	Homo sapiens
pmid	sentence
9837959	Using transiently transfected human embryonic kidney fibroblasts (HEK293), we demonstrate here that PLD1 activity, and to a lesser extent PLD2 activity, is stimulated in response to epidermal growth factor (EGF). PLD2, but not PLD1, associates with the EGF receptor in a ligand-independent manner and becomes tyrosine-phosphorylated upon EGF receptor activation. Tyrosine 11 (Tyr-11) of PLD2 was identified as the specific phosphorylation site. Mutation of this residue to phenylalanine enhanced basal activity almost 2-fold

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251097	Tyr192	HTETKSLyPSSEIQL	in vitro
pmid	sentence
11687594	Another major tyrosine phosphorylation site of STAM2 was identified as Tyr-192

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-167646	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
SIGNOR-167650	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184379	Tyr199	AFLASPEyVNLPING	Homo sapiens	Breast Cancer Cell
pmid	sentence
19254954	Taken together, these results and those of the ms/ms analyses confirmed tyr-3, tyr-7, and tyr-198 to be primary residues phosphorylated by egfr in the gstp1 protein. The phosphorylation increased gstp1 enzymatic activity significantly,

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184383	Tyr4	yTVVYFPV	Homo sapiens	Breast Cancer Cell
pmid	sentence
19254954	Taken together, these results and those of the ms/ms analyses confirmed tyr-3, tyr-7, and tyr-198 to be primary residues phosphorylated by egfr in the gstp1 protein. The phosphorylation increased gstp1 enzymatic activity significantly,

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-184387	Tyr8	MPPYTVVyFPVRGRC	Homo sapiens	Breast Cancer Cell
pmid	sentence
19254954	Taken together, these results and those of the ms/ms analyses confirmed tyr-3, tyr-7, and tyr-198 to be primary residues phosphorylated by egfr in the gstp1 protein. The phosphorylation increased gstp1 enzymatic activity significantly,

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235738	Tyr209	TGMFPRNyVTPVNRN	Homo sapiens	A-431 Cell
pmid	sentence
11726515	Phosphorylation of grb2 by bcr/abl or egf receptor reduced its sh3-dependent binding to sos in vivo, but not its sh2-dependent binding to bcr/abl. Tyr209 within the c-terminal sh3 domain of grb2 was identified as one of the tyrosine phosphorylation sites

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, EGFR Signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Noonan syndrome, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, SARS-CoV MAPK PERTURBATION

Identifier	Residue	Sequence	Organism
SIGNOR-202776	Tyr21	IENEEQEyVQTVKSS	Homo sapiens
pmid	sentence
24103589	The authors identified several phosphorylated residues by a combination of peptide mapping and sequence analysis and showed that recombinant pp60c-src phosphorylates annexin a1 near its amino terminus, at tyrosine 21 (tyr21). Also polyoma virus middle t/pp60c-src complex, recombinant pp50v-abl, and the egf receptor/kinase phosphorylated the same tyrosine residue. It was also shown that serine 27 residue of anxa1 is the primary site phosphorylated by protein kinase c (pkc). In the same study, the threonine 41 residue has been identified as a pkc substrate as well. The adenosine cyclic 3_,5_-phosphate dependent protein kinase a (pka) phosphorylates anxa1 in its carboxyl-terminal core at the threonine 216 residue (thr216) [2].Finally in 2013 caron et al. showed the relevance of y21 phosphorylation for the anxa1 stability. In fact the authors demonstrated that the tyrosine 21 phosphorylation is crucial for anxa1 sumoylation induced by egf

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-150852	Tyr211	QLTFALRyLNFFTKA	Homo sapiens	Breast Cancer Cell
pmid	sentence
17115032	Here, we show that the chromatin-bound pcna protein is phosphorylated on tyr 211, which is required for maintaining its function on chromatin and is dependent on the tyrosine kinase activity of egf receptor (egfr) in the nucleus. Phosphorylation on tyr 211 by egfr stabilizes chromatin-bound pcna protein and associated functions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262850	Tyr217	MAEEKKAyKKAKERE	Homo sapiens	HeLa Cell
pmid	sentence
19059208	We also detected tyrosine phosphorylation of Ymer by EGF stimulation as previously reported (Fig. 1A). Furthermore, we verified that EGF receptor-mediated tyrosine phosphorylation of Ymer is inhibited by AG1478, which is known as an EGF receptor tyrosine kinase inhibitor (Fig. 1B). A luciferase reporter assay showed that mutation of tyrosines on Ymer (YmerY217/279/304F) results in loss of the inhibitory activity for NF-kappaB signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262851	Tyr279	TDGEDADyTHFTNQQ	Homo sapiens	HeLa Cell
pmid	sentence
19059208	We also detected tyrosine phosphorylation of Ymer by EGF stimulation as previously reported (Fig. 1A). Furthermore, we verified that EGF receptor-mediated tyrosine phosphorylation of Ymer is inhibited by AG1478, which is known as an EGF receptor tyrosine kinase inhibitor (Fig. 1B). A luciferase reporter assay showed that mutation of tyrosines on Ymer (YmerY217/279/304F) results in loss of the inhibitory activity for NF-kappaB signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262852	Tyr304	SSHKGFHyKH	Homo sapiens	HeLa Cell
pmid	sentence
19059208	We also detected tyrosine phosphorylation of Ymer by EGF stimulation as previously reported (Fig. 1A). Furthermore, we verified that EGF receptor-mediated tyrosine phosphorylation of Ymer is inhibited by AG1478, which is known as an EGF receptor tyrosine kinase inhibitor (Fig. 1B). A luciferase reporter assay showed that mutation of tyrosines on Ymer (YmerY217/279/304F) results in loss of the inhibitory activity for NF-kappaB signaling.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273910	Tyr218	GDGSDHPyYNSIPSK	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-273912	Tyr219	DGSDHPYyNSIPSKM	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-273911	Tyr283	RQGSSDIySTPEGKL	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-273922	Tyr301	PTGEAPTyVNTQQIP	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251091	Tyr221	GGPEPGPyAQPSVNT	Homo sapiens	HEK-293 Cell
pmid	sentence
9642287	To address these questions, we have developed an antibody that specifically recognizes the CrkII protein phosphorylated on Tyr221, and we found that the EGF receptor directly phosphorylates CrkII on Tyr221. Furthermore, we observed that the phosphorylation of Tyr221 of CrkII correlated with its dissociation from the EGF receptor, implicating the phosphorylation of Tyr221 in the negative feedback of binding to the EGF receptor.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251092	Tyr228	YPGGSDNyGSLSRVT	Homo sapiens	A-431 Cell
pmid	sentence
14996911	In A431 cells, epidermal growth factor induced striking p120 phosphorylation at Y228. Y228-phosphorylated p120 localized to adherens junctions and lamellipodia, and was significantly enhanced in cells around the colony periphery.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276322	Tyr234	YMTQEGEyLPLDQRD	in vitro
pmid	sentence
21486282	These results demonstrate that the EGF receptor tyrosine kinase up-regulates the K(IR) 2.3 channel via phosphorylation of the Y234 residue of the WT protein.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236400	Tyr285	TEADGELyVFNTPSG	Homo sapiens	Glioblastoma Cell, A-431 Cell
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236396	Tyr406	DASSQDCyDIPRAFP	Homo sapiens	Glioblastoma Cell, A-431 Cell
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236420	Tyr447	SEELDENyVPMNPNS	Homo sapiens	Glioblastoma Cell, A-431 Cell
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236392	Tyr627	KGDKQVEyLDLDLDS	Homo sapiens	Glioblastoma Cell, A-431 Cell
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236404	Tyr659	VADERVDyVVVDQQK	Homo sapiens	Glioblastoma Cell, A-431 Cell
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Publications:

5

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, Hepatocellular Tumor, Noonan syndrome, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-233233	Tyr307	MRHVSISyDIPPTPG	in vitro
pmid	sentence
10734310	Gab1 is also phosphorylated in response to epidermal growth factor (egf) but is unable to induce tubule formation. nine tyrosines are phosphorylated by both receptors. Three of them (y307, y373, y407) bind phospholipase c-gamma (plc-gamma).

Identifier	Residue	Sequence	Organism
SIGNOR-236408	Tyr373	ASDTDSSyCIPTAGM	Homo sapiens
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236412	Tyr472	EPIQEANyVPMTPGT	Homo sapiens	Glioblastoma Cell, A-431 Cell
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236416	Tyr589	SHDSEENyVPMNPNL	Homo sapiens	Glioblastoma Cell, A-431 Cell
pmid	sentence
9890893	Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689).

Publications:

4

Organism:

In Vitro, Homo Sapiens

Pathways:

EGFR Signaling, Hepatocellular Tumor, Noonan syndrome, PI3K/AKT Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-86689	Tyr329	IDPELARyLNRNYWE	Homo sapiens
pmid	sentence
12953068	We have analysed hrs phosphorylation in response to epidermal growth factor (egf) stimulation and show that the evolutionary conserved tyrosines y329 and y334 provide the principal phosphorylation sitesover-expression of wild-type hrs or a double mutant, y329/334f, defective in egf-dependent phosphorylation, substantially retard egf receptor (egfr) degradation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-100246	Tyr334	ARYLNRNyWEKKQEE	Homo sapiens
pmid	sentence
12953068	We have analysed hrs phosphorylation in response to epidermal growth factor (egf) stimulation and show that the evolutionary conserved tyrosines y329 and y334 provide the principal phosphorylation sitesover-expression of wild-type hrs or a double mutant, y329/334f, defective in egf-dependent phosphorylation, substantially retard egf receptor (egfr) degradation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272234	Tyr34	FAAKMPRyRGAALAR	Homo sapiens	Hep-G2 Cell
pmid	sentence
23776207	How ACAP4 regulates membrane dynamics and curvature in response to EGF stimulation is unknown. Here, we show that phosphorylation of the N-terminal region of ACAP4, named the Bin, Amphiphysin, and RSV161/167 (BAR) domain, at Tyr34 is necessary for EGF-elicited membrane remodeling. \|EGF stimulation of cells causes phosphorylation of ACAP4 at Tyr34, which subsequently promotes ACAP4 homodimer curvature.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-133215	Tyr354	LMLRLQDyEEKTKKA	Homo sapiens	A-431 Cell
pmid	sentence
15647376	Ezrin was initially identified as a substrate for tyrosine phosphorylation by egfr (bretscher, 1989) and phosphorylation of residues y145 and y353 were detected to high stoichiometry after egf treatment . Phosphorylation of ezrin at y353 has been delineated to signal survival during epithelial cell differentiation via the phosphatidylinositol 3-kinase (pi3k)/akt pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262857	Tyr37	VPPGLDEyNPFSDSR	in vitro
pmid	sentence
9658162	In our efforts to identify cellular tyrosine kinases that phosphorylate SCAMPs, we are quite intrigued by the observation that among a number of kinases, only the EGFR exhibits activity toward SCAMPs. EGF catalyzes the progressive phosphorylation of the SCAMPs up to 1 h poststimulation and may enhance colocalization of the EGFR and SCAMP3 within the cell interior. EGF also induces SCAMP-EGFR association, as detected by coimmunoprecipitation, and phosphorylation of SCAMP3 is stimulated by the EGFR in vitro. These results suggest that phosphorylation of SCAMPs, either directly or indirectly, may be functionally linked to the internalization/down-regulation of the EGFR. we have observed that there are two tyrosines conserved in SCAMP1 and SCAMP3, which are not found in SCAMP2. Of these two tyrosines (Tyr37 and Tyr73 in SCAMP1; Tyr 41 and Tyr83 in SCAMP3), we consider Tyr37/41 to be a more likely site for tyrosine phosphorylation

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276872	Tyr370	SLEISQSyTTTQRES	in vitro
pmid	sentence
25601159	Here, we show that upon irradiation stimulation, ATM associates with and is phosphorylated by epidermal growth factor receptor (EGFR) at Tyr370 (Y370) at the site of DNA double-strand breaks.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252091	Tyr394	KKVSSTHyYLLPERP	Mus musculus	NIH-3T3 Cell
pmid	sentence
26280531	"here we found that the epidermal growth factor receptor (EGFR) phosphorylates Mig6 on Y394 and that this phosphorylation is primed by prior phosphorylation of an adjacent residue, Y395, by Src."

Publications:

1

Organism:

Mus Musculus

Pathways:

EGFR Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-262858	Tyr41	QYATLDVyNPFETRE	in vitro
pmid	sentence
9658162	In our efforts to identify cellular tyrosine kinases that phosphorylate SCAMPs, we are quite intrigued by the observation that among a number of kinases, only the EGFR exhibits activity toward SCAMPs. EGF catalyzes the progressive phosphorylation of the SCAMPs up to 1 h poststimulation and may enhance colocalization of the EGFR and SCAMP3 within the cell interior. EGF also induces SCAMP-EGFR association, as detected by coimmunoprecipitation, and phosphorylation of SCAMP3 is stimulated by the EGFR in vitro. These results suggest that phosphorylation of SCAMPs, either directly or indirectly, may be functionally linked to the internalization/down-regulation of the EGFR. we have observed that there are two tyrosines conserved in SCAMP1 and SCAMP3, which are not found in SCAMP2. Of these two tyrosines (Tyr37 and Tyr73 in SCAMP1; Tyr 41 and Tyr83 in SCAMP3), we consider Tyr37/41 to be a more likely site for tyrosine phosphorylation

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251096	Tyr41	QYATLDVyNPFETRE	in vitro
pmid	sentence
9658162	SCAMP3 Is Tyrosine Phosphorylated by EGFR in Vitro

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277500	Tyr433	AALDTIQySKHPPPL	Homo sapiens
pmid	sentence
31931029	Here we found that EGFR-stimulated phosphorylation of SQSTM1 at tyrosine 433 induces dimerization of its UBA domain, which disturbs the sequestration function of SQSTM1 and causes autophagic flux blocking.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-21875	Tyr460	TVDGKEIyNTIRRKT	Homo sapiens
pmid	sentence
1850098	We conclude that tyr-460 is a site of gap tyrosine phosphorylation by the egf receptor in vitro and likely in vivo. Gap tyr-460 is located immediately c terminal to the second gap sh2 domain, suggesting that its phosphorylation might have a role in regulating protein-protein interactions.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glioblastoma Multiforme

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265083	Tyr56	HNIVFGDyTWTEFDE	Homo sapiens	HEK-293 Cell
pmid	sentence
32860853	Reciprocally, TRIP13 was phosphorylated at tyrosine(Y) 56 by EGFRvIII and EGF-activated EGFR. Abrogating TRIP13 Y56 phosphorylation dramatically attenuated TRIP13 expression-enhanced EGFR signaling and GBM cell growth.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-162431	Tyr570	SSNFDSIyICPSTFA	Homo sapiens
pmid	sentence
20029029	A negative feedback loop consisting of egfr-mediated phosphorylation of hdac6 tyr(570) resulted in reduced deacetylase activity and increased acetylation of alpha-tubulin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273637	Tyr593	PIDWGEEySNSGGGG	Homo sapiens	U-251MG Cell
pmid	sentence
26721396	We demonstrate here that activated EGFR phosphorylates the Y593 residue of the protein known as family with sequence similarity 129, member B (FAM129B), which is overexpressed in many types of human cancer. FAM129B phosphorylation increased the interaction between FAM129B and Ras, resulting in reduced binding of p120-RasGAP to Ras.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-52950	Tyr66	LHQEDNDyINASLIK	Homo sapiens
pmid	sentence
9355745	After binding to egfr, ptp1b becomes tyrosine-phosphorylated at tyr-66 phosphorylation of ptp1b by egfr enhances its catalytic activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-20452	Tyr660	RLDGENIyIRHSNLM	Homo sapiens
pmid	sentence
1647028	The phosphorylation site has been localized to the 8-kda domain, which has one tyrosine, tyrosine-418. The 8-kda region is required for the assembly of the spectrin/actin complex, and phosphorylation by egfr reduced the ability of protein 4.1 to promote the assembly of the spectrin/actin/protein 4.1 ternary complex

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251098	Tyr699	TAKAVDGyVKPQIKQ	Homo sapiens	HEK-293 Cell, Breast Cancer Cell Line
pmid	sentence
11751923	We have shown that EGF activates STAT5b not only in a HEK293 cell model in which the EGFR is stably overexpressed but also in the MDA-MB468 breast cancer cell line. Furthermore, EGF (but not GH) is able to activate tyrosine phosphorylation of a Tyr-699 mutant of STAT5b. \| Fig. 2 A (bottom panels) demonstrates that EGF-induced phosphorylation of tyrosine 699 (the well-described site of STAT5b phosphorylation) is detected only in the EGFR-overexpressing MDA-MB468 cells and not the MCF-7 cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-113393	Tyr725	AGGGSATyMDQAPSP	Homo sapiens
pmid	sentence
11751923	Novel activation of stat5b in response to epidermal growth factor. novel activation of stat5b in response to epidermal growth factor.

Identifier	Residue	Sequence	Organism
SIGNOR-113397	Tyr740	AVCPQAHyNMYPQNP	Homo sapiens
pmid	sentence
11751923	Novel activation of stat5b in response to epidermal growth factor. novel activation of stat5b in response to epidermal growth factor.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-113401	Tyr743	PQAHYNMyPQNPDSV	Homo sapiens	HEK-293 Cell, Breast Cancer Cell
pmid	sentence
11751923	Novel activation of stat5b in response to epidermal growth factor. novel activation of stat5b in response to epidermal growth factor.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-22455	Tyr8	MTDVETTyADFIASG	Homo sapiens
pmid	sentence
1956339	The difference in inhibitory potency between pki_ and pki_ has been attributed to the absence of a tyrosine residue (tyr7) in pki_ that is present in the nh2-terminal region of pki_. This suggests that the absence of a single amino acid residue can result in variations in how the catalytic subunit of camp-dependent protein kinase interacts with pki which ultimately can result in alterations in pki inhibitory potency.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-203311	Tyr849	NFANFSAyPSEEDMI	Homo sapiens
pmid	sentence
24269888	Earlier studies have shown that eps15 at tyr-849 is phosphorylated in egf-stimulated cells and partly controls the internalization of mono-ubiquitinated egfr via uim domains of eps15 [10]. It has also been shown that active egfr phosphorylates tyr-849 directly;

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262856	Tyr971	TQQTEEQyFQFLAKF	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
22337768	In this study, we demonstrate that EGFR regulates the kinase activity of LRRK1 via tyrosine phosphorylation and that this is required for proper endosomal trafficking of EGFR. Phosphorylation of LRRK1 at Tyr-944 results in reduced LRRK1 kinase activity.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Organism
SIGNOR-121953		Homo sapiens
pmid	sentence
14967450	Betacellulin is synthesized primarily as a transmembrane precursor, which is then processed to mature molecule by proteolytic events;ten growth factors and their erbb specificities are depicted: egf, amphiregulin((ar), and tgfalfa bind erbb-1, betacellulin, heparin binding egf-like growth factor, and epiregulin bing both erbb-1 and erbb-4.

Identifier	Residue	Organism
SIGNOR-200813		Homo sapiens
pmid	sentence
23382875	Betacellulin is synthesized primarily as a transmembrane precursor, which is then processed to mature molecule by proteolytic events;ten growth factors and their erbb specificities are depicted: egf, amphiregulin((ar), and tgfalfa bind erbb-1, betacellulin, heparin binding egf-like growth factor, and epiregulin bing both erbb-1 and erbb-4.

Identifier	Residue	Organism
SIGNOR-67003		Homo sapiens
pmid	sentence
10209155	Betacellulin is synthesized primarily as a transmembrane precursor, which is then processed to mature molecule by proteolytic events;ten growth factors and their erbb specificities are depicted: egf, amphiregulin((ar), and tgfalfa bind erbb-1, betacellulin, heparin binding egf-like growth factor, and epiregulin bing both erbb-1 and erbb-4.

Identifier	Residue	Organism	Cell Line
SIGNOR-56365		Homo sapiens	Breast Cancer Cell
pmid	sentence
9528863	Betacellulin is synthesized primarily as a transmembrane precursor, which is then processed to mature molecule by proteolytic events;ten growth factors and their erbb specificities are depicted: egf, amphiregulin((ar), and tgfalfa bind erbb-1, betacellulin, heparin binding egf-like growth factor, and epiregulin bing both erbb-1 and erbb-4.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-255430		Homo sapiens
pmid	sentence
10029407	p53 transcriptionally activates expression of the genes encoding epidermal growth factor receptor, matrix metalloproteinase (MMP)-2, cathepsin D, and thrombospondin-1 but represses expression of the genes encoding basic fibroblast growth factor and multidrug resistance-1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Organism
SIGNOR-121965		Homo sapiens
pmid	sentence
14967450	The transcription factors stat1, stat3, and stat5 are directly phosphorylated by erbb-1, subsequent to which they dimerize through phosphotyrosine-sh2 domain interactions and translocate to the nucleus to activate gene trascription critical for proliferation.

Identifier	Residue	Organism	Cell Line
SIGNOR-235692		Homo sapiens	Breast Cancer Cell
pmid	sentence
22693070	The transcription factors stat1, stat3, and stat5 are directly phosphorylated by erbb-1, subsequent to which they dimerize through phosphotyrosine-sh2 domain interactions and translocate to the nucleus to activate gene trascription critical for proliferation.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Organism	Cell Line
SIGNOR-236327		in vitro	HeLa Cell
pmid	sentence
16729043	We determined interaction partners to all cytosolic tyrosine residues of the four members of the ErbB-receptor family in an unbiased fashion by quantitative proteomics using pull-down experiments with pairs of phosphorylated and nonphosphorylated synthetic peptides. Each receptor had characteristic preferences for interacting proteins and most interaction partners had multiple binding sites on each receptor. EGFR and ErbB4 had several docking sites for Grb2, while ErbB3 was characterized by six binding sites for PI3K.

Identifier	Residue	Organism	Cell Line
SIGNOR-235721		Mus musculus	NIH-3T3 Cell
pmid	sentence
7518560	Erbb1 recruites grb2 through sh2 domain;from these studies, we concluded that grb2 binds directly to the egfr at y-1068, to a lesser extent at y-1086, and indirectly at y-1173. Egfr has six binding sites for the adapter protein grb2, and erbb4 has five, each with different binding strength several tyrosine-based motifs recruit a number of signal transducers to the phosphorylated form of erbb1 such as the adaptor proteins growth-factor-receptor bound-2 (grb2) and src-homology-2-containing (shc).

Identifier	Residue	Organism
SIGNOR-267725		Homo sapiens
pmid	sentence
24697349	Adaptor protein Grb2 binds phosphotyrosines in the epidermal growth factor (EGF) receptor (EGFR) and thereby links receptor activation to intracellular signaling cascades.

Publications:

3

Organism:

In Vitro, Mus Musculus, Homo Sapiens

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, EGFR Signaling, Glioblastoma Multiforme, Hepatocellular Tumor, Noonan syndrome, Non-small-cell lung cancer (NSCLC), PI3K/AKT Signaling, SARS-CoV MAPK PERTURBATION

Identifier	Residue	Organism	Cell Line
SIGNOR-252671		Homo sapiens	MCF-7 Cell
pmid	sentence
26918608	P85alpha promotes nucleolin transcription and subsequently enhances EGFR mRNA stability and EGF-induced malignant cellular transformation.

Identifier	Residue	Organism
SIGNOR-252672		Homo sapiens
pmid	sentence
14967450	The egf-r coimmunoprecipitated with p85 alpha

Publications:

2

Organism:

Homo Sapiens

Tissue:

Breast Cancer Cell

Pathways:

Acute Myeloid Leukemia, COVID-19 Causal Network, FLT3-ITD in AML, Hepatocellular Tumor, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling

Identifier	Residue	Organism
SIGNOR-191009		Homo sapiens
pmid	sentence
Other

Identifier	Residue	Organism	Cell Line
SIGNOR-76554		Homo sapiens	A-431 Cell, CACO-2 Cell
pmid	sentence
10753475	Quinazoline analogues with 7-alkoxyamine solubilizing s were potent irreversible inhibitors of the isolated egfr enzyme, with ic(50[app]) values from 2 to 4 nm, and potently inhibited both egfr and erbb2 autophosphorylation in cells.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252076		in vitro
pmid	sentence
18046415	The cytoplasmic protein MIG6 (mitogen-induced gene 6; also known as ERRFI1) interacts with and inhibits the kinase domains of EGFR and ERBB2

Publications:

1

Organism:

In Vitro

Pathways:

EGFR Signaling

Identifier	Residue	Organism
SIGNOR-258254		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

Identifier	Residue	Organism
SIGNOR-121962		Homo sapiens
pmid	sentence
14967450	The transcription factors stat1, stat3, and stat5 are directly phosphorylated by erbb-1, subsequent to which they dimerize through phosphotyrosine-sh2 domain interactions and translocate to the nucleus to activate gene trascription critical for proliferation

Identifier	Residue	Organism
SIGNOR-235689		Homo sapiens
pmid	sentence
22693070	The transcription factors stat1, stat3, and stat5 are directly phosphorylated by erbb-1, subsequent to which they dimerize through phosphotyrosine-sh2 domain interactions and translocate to the nucleus to activate gene trascription critical for proliferation

Publications:

2

Organism:

Homo Sapiens

Pathways:

EGFR Signaling

Identifier	Residue	Organism
SIGNOR-149089		Homo sapiens
pmid	sentence
16932740	In conclusion, the use of pharmacological agents suggests that p38 mapk is the enzyme involved in egfr phosphorylation, as well as internalization, following exposure of cells to various stress-inducing conditions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-272104		Homo sapiens	HeLa Cell
pmid	sentence
23418353	RNF126 and Rabring7 associate with the EGFR through a ubiquitin-binding zinc finger domain and both E3 ubiquitin ligases promote ubiquitylation of EGFR. In HeLa cells depleted of either RNF126 or Rabring7 the EGFR is retained in a late endocytic compartment and is inefficiently degraded.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-107750		Homo sapiens
pmid	sentence
11350724	Shc exists in three different isoforms, p46shc, p52shc and p66shc which are tyrosine phosphorylated upon egf stimulation and bind to the activated egfr and grb2. Interestingly, while the 46 and 52 kda isoforms increase mitogenic signalling after egf stimulation and are able to transform nih3t3 cells (pelicci et al. 1992), p66shc has no transforming potential and negatively influences egf-induced c-fos transcription

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258306		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

Identifier	Residue	Organism	Cell Line
SIGNOR-272103		Homo sapiens	HeLa Cell
pmid	sentence
23418353	RNF126 and Rabring7 associate with the EGFR through a ubiquitin-binding zinc finger domain and both E3 ubiquitin ligases promote ubiquitylation of EGFR. In HeLa cells depleted of either RNF126 or Rabring7 the EGFR is retained in a late endocytic compartment and is inefficiently degraded.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-205936		Homo sapiens
pmid	sentence
Other

Identifier	Residue	Organism
SIGNOR-200902		Homo sapiens
pmid	sentence
23405260	The goal of this study was to compare dacomitinib (pf-00299804), a next generation small molecule tyrosine kinase inhibitor that irreversibly blocks multiple her family receptors (her-1 (egfr), her-2 and her-4 tyrosine kinases), to cetuximab, the current fda approved anti-egfr medication for hnscc and erlotinib, an egfr specific small molecule tyrosine kinase inhibitor.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-114701		Homo sapiens
pmid	sentence
11823423	Consistent with a negative role for c-Cbl, here we report that defective Tyr1045 of EGFR, an inducible c-Cbl docking site, enhances the mitogenic response to EGF

Identifier	Residue	Organism
SIGNOR-147826		Homo sapiens
pmid	sentence
16829981	Likewise, cbl is recruited to erbb1 either directly (tyr1045), or indirectly, trough grb2

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Glioblastoma Multiforme

Identifier	Residue	Organism	Cell Line
SIGNOR-109804		Homo sapiens	Glioblastoma Cell
pmid	sentence
11514572	Tc45 dephosphorylated delta egfr in u87mg glioblastoma cells and inhibited mitogen-activated protein kinase erk2 and phosphatidylinositol 3-kinase signaling. In contrast, the substrate-trapping tc45-d182a mutant, which is capable of forming stable complexes with tc45 substrates, suppressed the activation of erk2 but not phosphatidylinositol 3-kinase. The activation results in reduced egfr phosphorylation after egf stimulation. Introduction of the alpha(1) cytoplasmic domain peptide into cells induces phosphatase activation and inhibits egf-induced cell proliferation and anchorage-independent growth of malignant cells.

Identifier	Residue	Organism
SIGNOR-132316		Homo sapiens
pmid	sentence
15592458	Here, we report that the 45-kda variant of the protein tyrosine phosphatase tcptp (tc45) can recognize delta egfr as a cellular substrate

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-262237		in vitro
pmid	sentence
24556163	This analysis revealed that QL47 also potently inhibits BMX with an IC50 of 6.7 nM but impressively displays more than 100-fold selectivity against EGFR, HER2, JAK3, BLK, TEC, and ITK that possess an equivalently placed cysteine

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-77195		Homo sapiens	A-431 Cell
pmid	sentence
10805725	The n-terminal region of pi3k-c2beta was found to selectively interact with the egf receptor in vitro, suggesting that it mediates the association of this pi3k with the receptor.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-64731		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

Identifier	Residue	Organism
SIGNOR-269876		Homo sapiens
pmid	sentence
11279155	These results demonstrate that egfr-erbb2 oligomers are potent activators of mapk and akt, and this signaling does not require egfr kinase activity

Publications:

1

Organism:

Homo Sapiens

Pathways:

Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Organism
SIGNOR-65576		Homo sapiens
pmid	sentence
10085134	The epidermal growth factor receptor (EGFR) mediates the actions of a family of bioactive peptides that include epidermal growth factor (EGF) and amphiregulin (AR)

Identifier	Residue	Organism
SIGNOR-236356		Homo sapiens
pmid	sentence
20513444	Remarkably, three members of the epidermal growth factor (egf) family (ereg, areg, and epgn) showed increased expression that was associated with elevated epidermal activation of the egf receptor (egfr) and stat3, a downstream effector of egfr signaling.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Skin

Pathways:

EGFR Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-266057		Mus musculus	NIH-3T3 Cell
pmid	sentence
14522076	GC-binding factor 2 (GCF2) is a transcriptional repressor that decreases activity of the epidermal growth factor receptor (EGFR) and other genes. \|Deletion mutants of GCF2 revealed that amino acids 429–528 are required for both DNA binding and repression of the EGFR promoter.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism	Cell Line
SIGNOR-236519		Homo sapiens	HEK-293 Cell
pmid	sentence
11375397	Cbl proteins function as ubiquitin protein ligases for the activated epidermal growth factor receptor and, thus, negatively regulate its activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, EGFR Signaling

Identifier	Residue	Organism
SIGNOR-165782		Homo sapiens
pmid	sentence
20513444	Remarkably, three members of the epidermal growth factor (egf) family (ereg, areg, and epgn) showed increased expression that was associated with elevated epidermal activation of the egf receptor (egfr) and stat3, a downstream effector of egfr signaling.

Identifier	Residue	Organism	Cell Line
SIGNOR-54351		Homo sapiens	Breast Cancer Cell
pmid	sentence
9419975	Chemical cross-linking experiments showed that [125i]epiregulin directly bound to each of egfr and erbb-4 but not to erbb-2 and erbb-3. remarkably, three members of the epidermal growth factor (egf) family (ereg, areg, and epgn) showed increased expression that was associated with elevated epidermal activation of the egf receptor (egfr) and stat3, a downstream effector of egfr signaling.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Skin

Identifier	Residue	Organism	Cell Line
SIGNOR-265084		Homo sapiens	HEK-293 Cell
pmid	sentence
32860853	Mechanistically, TRIP13 enhanced EGFR protein abundance in part by preventing Cbl-mediated ubiquitination and proteasomal degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-151271		Homo sapiens	Leukemia Cell
pmid	sentence
17178722	This study shows that the anti-cancer drug erlotinib (tarceva) is a potent inhibitor of jak2(v617f) activity.

Identifier	Residue	Organism
SIGNOR-191502		Homo sapiens
pmid	sentence
Other

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-266352		Homo sapiens	MCF-7 Cell
pmid	sentence
21822308	We find that CHKA forms a complex with EGFR in a c-Src-dependent manner. Endogenous CHKA and EGFR co-immunoprecipitated from a variety of breast cancer cell lines and immortalized mammary epithelial cells. CHKA interacted with the EGFR kinase domain upon c-Src co-overexpression and was phosphorylated in a c-Src-dependent manner on Y197 and Y333. CHKA is required for maximum EGF-dependent cell growth in mammary epithelium-derived cell lines

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-272604		Chlorocebus aethiops	COS-1 Cell
pmid	sentence
12226085	In summary, we have shown that CBLC and AIP4 can interact and that these two E3 ligases could contribute to down-regulate EGFR signaling by ubiquitination.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Organism	Cell Line
SIGNOR-259890		Homo sapiens	Colorectal Cancer Cell
pmid	sentence
16336752	Cetuximab binds to domain III of EGFR and hinders ligand binding. It is now approved by the US Food and Drug Administration for metastatic colorectal cancer treatment.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190467		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-191145		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258234		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

Identifier	Residue	Organism
SIGNOR-189900		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-189033		Homo sapiens
pmid	sentence
19882665	We show that egfr-mediated signaling promotes sox2 expression, which in turn binds to the egfr promoter and directly upregulates egfr expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-272934		Homo sapiens
pmid	sentence
10542134	Here we describe that overexpression of cbl-b, a homologue of the c-cbl protooncogene, inhibits EGFR-induced apoptosis in MDA-MB-468 breast cancer cells. Overexpression of cbl-b results in a shortened duration of EGFR activation upon EGF stimulation. This is demonstrated by decreased amounts of phosphorylated EGFR as well as by inhibition of multiple downstream signaling pathways. The inhibition of signaling by cbl-b results from increased ubiquitination and degradation of the activated EGFR.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, EGFR Signaling

Identifier	Residue	Organism
SIGNOR-197959		Homo sapiens
pmid	sentence
22722787	Xl647 is an oral small-molecule inhibitor of multiple receptor tyrosine kinases, including endothelial growth factor receptor (egfr), vascular endothelial growth factor receptor 2, her2 and ephrin type-b receptor 4 (ephb4).

Identifier	Residue	Organism
SIGNOR-207857		Homo sapiens
pmid	sentence
Other

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-55861		Homo sapiens	Neuron
pmid	sentence
24212772	Several tyrosine-based motifs recruit a number of signal transducers to the phosphorylated form of erbb1 such as the adaptor proteins growth-factor-receptor bound-2 (grb2) and src-homology-2-containing (shc).

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Organism
SIGNOR-186159		Homo sapiens
pmid	sentence
12297050	Epidermal growth factor (egf) regulates cell proliferation and differentiation by binding to the egf receptor (egfr) extracellular region, comprising domains i-iv, with the resultant dimerization of the receptor tyrosine kinase.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, EGFR Signaling, Glioblastoma Multiforme, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, SARS-CoV MAPK PERTURBATION

Identifier	Residue	Organism
SIGNOR-189356		Homo sapiens
pmid	sentence
Other

Identifier	Residue	Organism	Cell Line
SIGNOR-196760		Homo sapiens	Lung Cancer Cell
pmid	sentence
22452896	Afatinib, an irreversible erbb-family blocker, has shown preclinical activity when tested in egfr mutant models with mutations that confer resistance to egfr tyrosine-kinase inhibitors.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-207827		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-262254		in vitro
pmid	sentence
20143778	By incorporating histone deacetylase (HDAC) inhibitory functionality into the pharmacophore of the epidermal growth factor receptor (EGFR) and human epidermal growth factor receptor 2 (HER2) inhibitors, we synthesized a novel series of compounds with potent, multiacting HDAC, EGFR, and HER2 inhibition and identified 7-(4-(3-ethynylphenylamino)-7-methoxyquinazolin-6-yloxy)-N-hydroxyheptanamide 8 (CUDC-101) as a drug candidate, which is now in clinical development. 8 displays potent in vitro inhibitory activity against HDAC, EGFR, and HER2 with an IC(50) of 4.4, 2.4, and 15.7 nM, respectively.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-146852		Homo sapiens
pmid	sentence
16729043	We identified stat5 as a direct binding partner to egfr and erbb4 and discovered new recognition motifs for shc and stat5.Egf stimulation and subsequent phosphorylation of egfr at tyrosine y978, y998 and y869 would then subsequently lead to recruitment and activation of stat5.

Identifier	Residue	Organism	Cell Line
SIGNOR-68159		Homo sapiens	A-431 Cell
pmid	sentence
10358079	We identified stat5 as a direct binding partner to egfr and erbb4 and discovered new recognition motifs for shc and stat5.Egf stimulation and subsequent phosphorylation of egfr at tyrosine y978, y998 and y869 would then subsequently lead to recruitment and activation of stat5.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, FLT3-ITD in AML

Identifier	Residue	Organism
SIGNOR-192623		Homo sapiens
pmid	sentence
Other

Identifier	Residue	Organism	Cell Line
SIGNOR-126976		Homo sapiens	Lung Cancer Cell
pmid	sentence
15329413	Egfr is a tk of the erbb family that is the presumptive target of the tk inhibitor (tki) gefitinib.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-194628		Homo sapiens
pmid	sentence
Other

Identifier	Residue	Organism	Cell Line
SIGNOR-153318		Homo sapiens	Lung Cancer Cell
pmid	sentence
17311002	However, the same cells were highly sensitive to the irreversible dual-specificity egfr/erbb2 kinase inhibitor hki-272, as were those overexpressing wild-type erbb2.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-189377		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-115988		Homo sapiens	Breast Cancer Cell
pmid	sentence
11897506	Gpcr-mediated transactivation of egfrs by estrogen provides a previously unappreciated mechanism of cross-talk between estrogen and serum growth factors, and explains prior data reporting the egf-like effects of estrogen

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190149		Homo sapiens
pmid	sentence
Other

Identifier	Residue	Organism
SIGNOR-163727		Homo sapiens
pmid	sentence
20145185	In vivo, azd8931 inhibited xenograft growth in a range of models while significantly affecting egfr, erbb2, and erbb3 phosphorylation and downstream signaling pathways, apoptosis, and proliferation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-205755		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-265954		Homo sapiens	HEK-293 Cell, HeLa Cell
pmid	sentence
27117702	Here we find that METTL3 promotes translation of certain mRNAs including epidermal growth factor receptor (EGFR) and the Hippo pathway effector TAZ in human cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-65642		Homo sapiens
pmid	sentence
20332299	Ligand binding to EGFR also leads to rapid internalization and proteosomal/lysosomal degradation of the receptors. This process results in a dramatic downregulation of both total and cell surface receptors. EGF-induced degradation of EGFR is thought to be initiated by phosphorylation of tyrosine 1045 of the receptor followed by binding of Cbl adaptor proteins and ubiquitination of the receptor. Internalized EGFR is transported to early endosomes where receptor-ligand complexes are sorted for either degradation or recycling to the cell surface.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, Glioblastoma Multiforme

Identifier	Residue	Organism	Cell Line
SIGNOR-259898		Homo sapiens	Carcinoma Cell
pmid	sentence
11255078	ABX-EGF binds EGFr with high affinity (5x10(-11) M), blocks the binding of both EGF and transforming growth factor-alpha (TGF-alpha) to various EGFr-expressing human carcinoma cell lines, and inhibits EGF-dependent tumor cell activation, including EGFr tyrosine phosphorylation, increased extracellular acidification rate, and cell proliferation. Being a fully human antibody, ABX-EGF is anticipated to exhibit a long serum half-life and minimal immunogenicity with repeated administration, even in immunocompetent patients. These results demonstrate the potent anti-tumor activity of ABX-EGF and its therapeutic potential for the treatment of multiple human solid tumors that overexpress EGFr.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-93199		Homo sapiens	Pancreatic Cancer Cell
pmid	sentence
16585207	Our data indicate that a subset of cell lines is dependent on TGF-_-mediated activation of the EGFR for cell proliferation and strongly suggest that pancreatic tumors expressing high levels of TGF-_ and phosphorylated (activated) EGFR are EGFR-dependent in vitro and in vivo.

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, Hepatocellular Tumor, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Organism
SIGNOR-106500		Homo sapiens
pmid	sentence
11279155	These results demonstrate that egfr-erbb2 oligomers are potent activators of mapk and akt, and this signaling does not require egfr kinase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277090		Homo sapiens
pmid	sentence
28065597	We further found that PTPRH and PTPRB directly dephosphorylate EGFR and repress its downstream signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-101530		Homo sapiens
pmid	sentence
12783862	The interaction between egfr and rin1 delineates a novel signal transduction pathway between egfr and its effectors, rin1, rab5a, and ras, which together coordinate and regulate both signaling and membrane trafficking.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-269264		Homo sapiens
pmid	sentence
15284455	Gefitinib (Iressa, Astra Zeneca Pharmaceuticals) is a tyrosine kinase inhibitor that targets the epidermal growth factor receptor (EGFR) and induces dramatic clinical responses in nonsmall cell lung cancers (NSCLCs) with activating mutations within the EGFR kinase domain.

Identifier	Residue	Organism
SIGNOR-258218		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:

Homo Sapiens, In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-271516		Homo sapiens	HEK-293 Cell
pmid	sentence
15590694	SOCS5 Can Physically Associate with the EGFR. The complex recruited by SOCS proteins is composed of ElonginBC, Cullin, and Roc1 (15, 16). Together, this complex has E3 ubiquitin ligase activity. We suspect that the role of the SB domain is to mediate coupling of EGFR with the Elongin-Cullin-Roc E3 ubiquitin ligase complex, resulting in enhanced EGFR degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-114167		Homo sapiens
pmid	sentence
11799118	We have previously shown that sh3px1, phosphorylated by ack2 (activated cdc42-associated tyrosine kinase 2), regulates the degradation of egf (epidermal growth factor) receptor.The cdc42 target ack2 interacts with sorting nexin 9 (sh3px1) to regulate epidermal growth factor receptor degradation.

Identifier	Residue	Organism
SIGNOR-142566		Homo sapiens
pmid	sentence
16316319	We have previously shown that sh3px1, phosphorylated by ack2 (activated cdc42-associated tyrosine kinase 2), regulates the degradation of egf (epidermal growth factor) receptor.The cdc42 target ack2 interacts with sorting nexin 9 (sh3px1) to regulate epidermal growth factor receptor degradation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277029		Homo sapiens
pmid	sentence
12018405	Some 10 years ago, Hashimoto et al. (87) had shown that the LAR catalytic domain can dephosphorylate the EGFR receptor in vitro, and more recently, Kulas and colleagues (88) have demonstrated that the antisense mediated suppression of LAR can enhance the growth factor induced activation of EGFR in rat hepatoma cells.\|These data indicate that LAR and RPTPsigma may have a significant role in GPCR induced EGFR signalling.Whereas in A431 cells LAR and RPTPsigma may act to suppress the EGFR in response to GPCR activation, it is possible that the converse may also be true in other cell types.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-147838		Homo sapiens
pmid	sentence
8816440	Although erbb-2 binds neither ligand, even in a heterodimeric receptor complex, it is the preferred heterodimer partner of the three other members, and it favors interaction with erbb-3.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-189942		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252089		Mus musculus	NIH-3T3 Cell
pmid	sentence
1333047	We show that epidermal growth factor or platelet-derived growth factor stimulation of intact human or murine cells leads to phosphorylation of Nck protein on tyrosine, serine, and threonine residues

Publications:

1

Organism:

Mus Musculus

Pathways:

EGFR Signaling

Identifier	Residue	Organism
SIGNOR-195248		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-107712		Homo sapiens
pmid	sentence
11350724	Adaptors such as Shc, Grb2, Crk or the recently characterised Dok-R protein (Jones Dumont 1999) show a modular structure containing protein protein interaction domains and putative phosphorylation sites and act as signalling platforms which extend the receptors repertoire of activated intracellular pathways.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, FLT3-ITD in AML, Noonan syndrome

Identifier	Residue	Organism
SIGNOR-73874		Homo sapiens
pmid	sentence
10618391	Oligomerization of receptor protein tyrosine kinases such as the epidermal growth factor receptor (egfr) by their cognate ligands leads to activation of the receptor.We Demonstrate that vav-2 is phosphorylated on tyrosine residues in response to egf and associates with the egfr in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-189036		Homo sapiens
pmid	sentence
19882665	We show that egfr-mediated signaling promotes sox2 expression, which in turn binds to the egfr promoter and directly upregulates egfr expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270017		Homo sapiens
pmid	sentence
1651322	It is likely that the map2 and ert kinases account for the phosphorylation of the egf receptor at thr669 (egf receptor (krel veplt669psgeapnqallr)) observed in cultured cells.Phosphorylation at ser-695 is partial and occurs only if thr-693 is phosphorylated. Phosphorylation at thr-678 and thr-693 by prkd1 inhibits egf-induced mapk8/jnk1 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-272220		Homo sapiens	BT-549 Cell
pmid	sentence
31801577	CGRRF1 ubiquitinates EGFR through K48-linked ubiquitination, which leads to proteasome degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252088		Homo sapiens
pmid	sentence
15284024	Stimulation of EGFR induces Tyr701 phosphorylation of STAT1 and initiates complex formation of STAT1 and STAT3 with JAK1 and JAK2. Thereafter, the STATs translocate to the nucleus within 15 min.

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, Pancreatic ductal adenocarcinoma (PDA)

Identifier	Residue	Organism	Cell Line
SIGNOR-271521		Homo sapiens	HEK-293 Cell
pmid	sentence
15590694	SOCS5 Can Physically Associate with the EGFR. The complex recruited by SOCS proteins is composed of ElonginBC, Cullin, and Roc1 (15, 16). Together, this complex has E3 ubiquitin ligase activity. We suspect that the role of the SB domain is to mediate coupling of EGFR with the Elongin-Cullin-Roc E3 ubiquitin ligase complex, resulting in enhanced EGFR degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-157867		Homo sapiens	Breast Cancer Cell
pmid	sentence
17892419	Recently, lapatinib, a small molecule dual inhibitor of both her2 and egf receptors, has been developed to expand the options for treating her-positive breast cancer.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-152805		Homo sapiens	Colonic Cancer Cell
pmid	sentence
17251915	Ep2 can also promote the transactivation of epidermal growth factor receptor (egfr) expressed in colon cancer cells through src, which activates the proteolytic release of the egfr ligands amphiregulin (ar) and transforming growth factor-alfa (tgfalfa).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258169		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

Identifier	Residue	Organism	Cell Line
SIGNOR-235655		Mus musculus	Keratinocyte
pmid	sentence
15284024	Two possibilities for STAT activation exist: a janus kinase (JAK)-dependent and a JAK-independent mechanism. Herein, we demonstrate that EGFR overexpression in primary esophageal keratinocytes activates STAT in a JAK-dependent fashion

Publications:

1

Organism:

Mus Musculus

Pathways:

COVID-19 Causal Network

Identifier	Residue	Organism
SIGNOR-114087		Homo sapiens
pmid	sentence
11788593	We show that retinoic acid receptor (rar)-selective ligands reduce egfr level and the magnitude and duration of egfr activation in egf-stimulated cells

Publications:

1

Organism:

Homo Sapiens

Pathways:

Acute Myeloid Leukemia

Identifier	Residue	Organism	Cell Line
SIGNOR-272605		Chlorocebus aethiops	COS-1 Cell
pmid	sentence
12226085	In summary, we have shown that CBLC and AIP4 can interact and that these two E3 ligases could contribute to down-regulate EGFR signaling by ubiquitination.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Organism
SIGNOR-189386		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258212		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

Identifier	Residue	Organism
SIGNOR-261692		Homo sapiens
pmid	sentence
30021164	Here, we demonstrate that COMMD5 is crucial for the stability of the cytoskeleton. Its silencing leads to a major re-organization of actin and microtubule networks. The N terminus of COMMD5 binds to the endosomal Rab5, and its C terminus, including the COMMD domain, binds to the cytoskeletal scaffolding. COMMD5 participates in long-range endosome transport, including epidermal growth factor receptor (EGFR) recycling, and provides the strength to deform and assist the scission of vesicles into sorting endosomes. This study establishes the molecular mechanism by which COMMD5 acts as an adaptor protein to coordinate endosomal trafficking and reveals its important role for EGFR transport and activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-22716		Homo sapiens
pmid	sentence
12648462	The mammalian ligands that bind the egf receptor (egfr [her1, erb-b1]) include egf, transforming growth factor- (tgf), heparin-binding egf-like growth factor (hb-egf), amphiregulin (ar), betacellulin (btc), epiregulin (epr), and epigen

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, EGFR Signaling, Glioblastoma Multiforme, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), PI3K/AKT Signaling, SARS-CoV MAPK PERTURBATION

Identifier	Residue	Organism	Cell Line
SIGNOR-259102		Homo sapiens	HeLa Cell
pmid	sentence
20736164	USP8 is known to deubiquitinate EGFR in response to ligand stimulation. USP8 depletion accelerates receptor turnover, whereas loss of hepatocyte growth factor-regulated substrate (Hrs) rescues this phenotype, indicating that USP8 protects EGFR from degradation via an Hrs-dependent pathway. [..]As EGFR stabilization against lysosomal turnover requires deubiquitination by USP8.

Identifier	Residue	Organism	Cell Line
SIGNOR-259103		Homo sapiens	HeLa Cell
pmid	sentence
16120644	Here, we describe the role of a deubiquitinating enzyme UBPY/USP8 in the down-regulation of epidermal growth factor (EGF) receptor (EGFR). Overexpression of UBPY reduced the ubiquitination level of EGFR and delayed its degradation in EGF-stimulated cells.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-185124		Homo sapiens
pmid	sentence
19351721	The removal of the epidermal growth factor receptor (egfr) from the cell surface by endocytosis is triggered by receptor activation, but many facets of egfr trafficking remain unresolvedthe ap-2 complex is involved in the internalization of activated egfr.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-243278		Cricetulus griseus	CHO-7 Cell
pmid	sentence
15383614	We suggest that the ubiquitinated EGFR or another c-Cbl substrate that is ubiquitinated upon EGFR activation recruits Eps15 to the plasma membrane via its UIM. This event would facilitate EGFR internalization via a clathrin-dependent route in which Eps15 plays a role

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Organism	Cell Line
SIGNOR-235870		Mus musculus	Keratinocyte
pmid	sentence
15284024	Two possibilities for STAT activation exist: a janus kinase (JAK)-dependent and a JAK-independent mechanism. Herein, we demonstrate that EGFR overexpression in primary esophageal keratinocytes activates STAT in a JAK-dependent fashion

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, EGFR Signaling

Identifier	Residue	Organism
SIGNOR-205716		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-259906		Homo sapiens
pmid	sentence
30683916	Collectively, our findings revealed a novel mechanism wherein MALAT1 interacts with c-MYC to transactivate KTN1 for enhancing EGFR protein expression, which finally contributes to the development of cSCC.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-121977		Homo sapiens
pmid	sentence
14967450	Ten growth factors and their erbb specificities are depicted: egf, amphiregulin((ar), and tgfalfa bind erbb-1, betacellulin, heparin binding egf-like growth factor, and epiregulin bing both erbb-1 and erbb-4

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-252073		Mus musculus	NR-6 Cell
pmid	sentence
20421427	We report here an additional mechanism of EGFR suppression mediated by RALT, demonstrating that RALT-bound EGF receptors undergo endocytosis and eventual degradation into lysosomes

Publications:

1

Organism:

Mus Musculus

Pathways:

EGFR Signaling

Identifier	Residue	Organism
SIGNOR-67000		Homo sapiens
pmid	sentence
10209155	ErbB ligands include: EGF, transforming growth factor (TGF)_, and amphiregulin which only bind ErbB1

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-33633		Homo sapiens	MCF-7 Cell
pmid	sentence
26918608	p85alpha promotes nucleolin transcription and subsequently enhances EGFR mRNA stability and EGF-induced malignant cellular transformation.

Identifier	Residue	Organism
SIGNOR-121959		Homo sapiens
pmid	sentence
14967450	The egf-r coimmunoprecipitated with p85 alpha

Publications:

2

Organism:

Homo Sapiens

Tissue:

Breast Cancer Cell

Pathways:

Glioblastoma Multiforme

Identifier	Residue	Organism
SIGNOR-166568		Homo sapiens
pmid	sentence
20626350	Such phosphorylation is required for tace mediated ectodomain shedding of tgfalfa family ligands, which results in the activation of egfr and cell proliferation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-269679		Homo sapiens
pmid	sentence
35220009	Interestingly, the O-GalNAcylation of EGFR, which is the key factor related to the metastasis cascade, was impacted by GALNT8. Furthermore, our results suggested that the GALNT8-mediated O-GalNAcylation led to the suppression of the EGFR signaling pathway and metastatic potential in breast cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-150190		Homo sapiens
pmid	sentence
17062696	The studies described here are intended to characterize the ability of bms-599626, a small-molecule inhibitor of the human epidermal growth factor receptor (her) kinase family, to modulate signaling and growth of tumor cells that depend on her1 and/or her2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-149086		Homo sapiens
pmid	sentence
16932740	P38 map kinase mediates stress-induced internalization of egfrthe underlying mechanism entails phosphorylation of egfr at a short segment (amino acids 1002-1022) containing multiple serines and threonines, as well as phosphorylation of two rab5 effectors, eea1 and gdi.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-52954		Homo sapiens
pmid	sentence
9362449	We found that nck does not directly bind to egf receptor, instead it binds via its sh2 domain to a 62 kda phosphotyrosine protein

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling

Identifier	Residue	Organism
SIGNOR-277130		Homo sapiens
pmid	sentence
20335174	Conversely, increasing expression of PTPN9 wild type (WT) inhibits tyrosyl phosphorylation of ErbB2 and EGFR.\|Protein-tyrosine phosphatase PTPN9 negatively regulates ErbB2 and epidermal growth factor receptor signaling in breast cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190050		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258196		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

Identifier	Residue	Organism
SIGNOR-165779		Homo sapiens
pmid	sentence
20513444	Remarkably, three members of the epidermal growth factor (egf) family (ereg, areg, and epgn) showed increased expression that was associated with elevated epidermal activation of the egf receptor (egfr) and stat3, a downstream effector of egfr signaling.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skin

Identifier	Residue	Organism	Cell Line
SIGNOR-235481		Mus musculus	NIH-3T3 Cell
pmid	sentence
7518560	Both competition experiments with synthetic phosphopeptides and dephosphorylation protection analysis demonstrated that y-1173 and y-992 are major and minor binding sites, respectively, for shc on the egfr.

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, FLT3-ITD in AML, Noonan syndrome

Identifier	Residue	Organism
SIGNOR-277145		Homo sapiens
pmid	sentence
12018405	Similarly, Pestana et al. (89) have reported that overexpression of RPTPsigma in human A431 carcinoma cells partially inhibits EGFR activation, whereas antisense mediated suppression of RPTPsigma expression enhances EGFR activation, substrate phosphorylation, and signalling.\|These data indicate that LAR and RPTPsigma may have a significant role in GPCR induced EGFR signalling.Whereas in A431 cells LAR and RPTPsigma may act to suppress the EGFR in response to GPCR activation, it is possible that the converse may also be true in other cell types.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-115734		Homo sapiens	Breast Cancer Cell
pmid	sentence
11887937	Activation of estrogen receptor-alpha (eralpha) by growth factors in the absence of estrogen is a well-documented phenomenon.Egfr tyrosine kinase in vitro stimulated the phosphorylation of recombinant er

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-251901		Homo sapiens
pmid	sentence
11875647	UVB increases keratin 5 and keratin 14 expression through direct activation of the EGF receptor in SVHK.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-266902		Homo sapiens	HeLa Cell
pmid	sentence
16520378	Degradation of acutely stimulated receptor tyrosine kinases, epidermal growth factor receptor and Met, is strongly inhibited in UBPY knockdown cells suggesting that UBPY function is essential for growth factor receptor down-regulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-262040		Homo sapiens	Prostate Cancer Cell Line
pmid	sentence
27477906	Our quantitative ChIP experiments confirmed that ZMYND8 and JARID1D were co-localized at Slug, CD44, VEGFA, and EGFR genes (Figures 4F–4I). Our ChIP results also showed that ZMYND8 repressed and occupied other JARID1D target genes, such as the matrix metalloproteinase 1 (MMP1) and MMP3, that we previously reported

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-186198		Rattus norvegicus
pmid	sentence
11003669	These data indicate that the gene 33 protein is a feedback inhibitor of ErbB-2 mitogenic function and a suppressor of ErbB-2 oncogenic activity. We propose that the gene 33 protein be renamed with the acronym RALT (receptor-associated late transducer)

Publications:

1

Organism:

Rattus Norvegicus

Pathways:

EGFR Signaling

Identifier	Residue	Organism
SIGNOR-252092		Mus musculus
pmid	sentence
26592448	Instead our data provide novel evidence that EGFR signaling is needed to activate the oncogenic and pro-proliferative transcription factor c-MYC

Publications:

1

Organism:

Mus Musculus

Pathways:

Acute Myeloid Leukemia, EGFR Signaling, FLT3-ITD in AML, Hepatocellular Tumor

Identifier	Residue	Organism
SIGNOR-182562		Homo sapiens
pmid	sentence
19054389	Epsin 1 is involved in recruitment of ubiquitinated egf receptors into clathrin-coated pits this supports the contention that epsin 1 promotes endocytosis of the ubiquitinated egfr.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-127304		Homo sapiens
pmid	sentence
15282549	Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skin

Name	EGFR View Modifications
Full Name	Epidermal growth factor receptor
Synonyms	Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1 \| ERBB, ERBB1, HER1
Primary ID	P00533
Links	- -
Type	protein
Relations	268
Pathways	Acute Myeloid Leukemia, COVID-19 Causal Network, EGFR Signaling, FLT3-ITD in AML, Glioblastoma Multiforme, Hepatocellular Tumor, Noonan syndrome, Non-small-cell lung cancer (NSCLC), Pancreatic ductal adenocarcinoma (PDA), SARS-CoV MAPK PERTURBATION
Inhibitors	canertinib; neratinib; vandetanib; dacomitinib; 9-(1-Methyl-4-pyrazolyl)-1-[1-(1-oxoprop-2-enyl)-2,3-dihydroindol-6-yl]-2-benzo[h][1,6]naphthyridinone; erlotinib hydrochloride; 873837-23-1; CUDC-101; lapatinib; VARLITINIB; XL-647; afatinib; WZ4002; gefitinib; tyrphostin AG 1478; sapitinib; pelitinib; N-[4-[3-chloro-4-[(3-fluorophenyl)methoxy]anilino]-6-quinazolinyl]-2-propenamide; OSI-420; tyrphostin B42; erlotinib; PD-153035 hydrochloride; BMS-599626; AV412
Function	Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536, PubMed:20837704, PubMed:17909029). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity).

The SIGnaling Network
Open Resource

Summary

Viewer

Search Tools

▶Modifications Tables

Relations