| + |
ERBB2 | up-regulates activity 
phosphorylation
|
SHCBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280009 |
Ser273 |
SSLSNCNsDSEQENI |
Homo sapiens |
|
| pmid |
sentence |
| 35013128 |
Blocking HER2 activation using trastuzumab effectively abolished EGF-induced nuclear localization of SHCBP1 in gastric cancer cells [7].|In addition, nuclear translocation of SHCBP1 is a downstream consequence of HER2 activation, which is dependent on phosphorylation of SHCBP1 at the Ser273 site. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates
phosphorylation
|
ERBB2 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181191 |
Thr686 |
QQKIRKYtMRRLLQE |
Homo sapiens |
|
| pmid |
sentence |
| 18799465 |
Pka directly phosphorylated erbb2 on thr-686, a highly conserved intracellular regulatory site that was required for the pka-mediated synergistic enhancement of neuregulin-induced erbb2-erbb3 activation and proliferation in scs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
ERBB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251129 |
Tyr1023 |
DLVDAEEyLVPQQGF |
Homo sapiens |
|
| pmid |
sentence |
| 1706616 |
Y1023 and Y1248, Y1139 and Y1222 also serve as autophosphorylation sites of HER2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251127 |
Tyr1139 |
TCSPQPEyVNQPDVR |
in vitro |
|
| pmid |
sentence |
| 1706616 |
Y1023 and Y1248, Y1139 and Y1222 also serve as autophosphorylation sites of HER2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251130 |
Tyr1222 |
PAFDNLYyWDQDPPE |
in vitro |
|
| pmid |
sentence |
| 1706616 |
Y1023 and Y1248, Y1139 and Y1222 also serve as autophosphorylation sites of HER2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251128 |
Tyr1248 |
PTAENPEyLGLDVPV |
in vitro |
|
| pmid |
sentence |
| 1706616 |
Y1023 and Y1248, Y1139 and Y1222 also serve as autophosphorylation sites of HER2. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, In Vitro |
| Pathways: | Colorectal Carcinoma |
| + |
PTPN11 | down-regulates 
dephosphorylation
|
ERBB2 |
0.834 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262957 |
Tyr1023 |
DLVDAEEyLVPQQGF |
in vitro |
|
| pmid |
sentence |
| 32024694 |
...which in turn suggests the importance SHP2 dephosphorylation of pTyr992 in EGFR and pTyr1023 in HER2 to mediate signaling.|More specifically, we show that acidic residues N-terminal to the substrate pTyr in EGFR and HER2 mediate specific binding by the SHP2 active site, leading to blockade of RasGAP binding and optimal signaling by the two receptors. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPN18 | down-regulates quantity by destabilization
dephosphorylation
|
ERBB2 |
0.665 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262595 |
Tyr1112 |
DPSPLQRySEDPTVP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25081058 |
PTPN18 knockdown selectively enhances the EGF-induced tyrosine phosphorylation of the HER2 Y1112, Y1196 and Y1248 sites. |Whereas the catalytic domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation of HER2 on pY(1112), the PEST domain of PTPN18 promotes K48-linked HER2 ubiquitination and its rapid destruction via the proteasome pathway and an HER2 negative feedback loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262596 |
Tyr1196 |
GAVENPEyLTPQGGA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25081058 |
PTPN18 knockdown selectively enhances the EGF-induced tyrosine phosphorylation of the HER2 Y1112, Y1196 and Y1248 sites. |Whereas the catalytic domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation of HER2 on pY(1112), the PEST domain of PTPN18 promotes K48-linked HER2 ubiquitination and its rapid destruction via the proteasome pathway and an HER2 negative feedback loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262597 |
Tyr1248 |
PTAENPEyLGLDVPV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25081058 |
PTPN18 knockdown selectively enhances the EGF-induced tyrosine phosphorylation of the HER2 Y1112, Y1196 and Y1248 sites. |Whereas the catalytic domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation of HER2 on pY(1112), the PEST domain of PTPN18 promotes K48-linked HER2 ubiquitination and its rapid destruction via the proteasome pathway and an HER2 negative feedback loop. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277031 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25081058 |
In the present study, we demonstrated that PTPN18 specifically dephosphorylates HER2 pY 1112, pY 1196 and pY 1248 sites among ten HER2 and EGFR C-terminal tyrosine phosphorylation sites (XREF_FIG).|Taken together, these data suggest that PTPN18 promotes the proteasome dependent degradation of HER2 through K48 linked polyubiquitination. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | down-regulates
phosphorylation
|
ERBB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21211 |
Tyr1112 |
DPSPLQRySEDPTVP |
Homo sapiens |
|
| pmid |
sentence |
| 1706616 |
However, each of these peptides contains tyrosines that correspond to major autophosphorylation sites of the epidermal growth factor receptor, suggesting that, in addition to y1023 and y1248, y1139 and y1222 also serve as autophosphorylation sites of her2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| Pathways: | Colorectal Carcinoma |
| + |
ERBB2 | up-regulates
phosphorylation
|
ERBB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124856 |
Tyr1196 |
GAVENPEyLTPQGGA |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15156151 |
Stimulation of these molecules, however, failed to induce efficient cell migration in the absence of neu/erbb2 phosphorylation at tyr 1201 or tyr 1227 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21199 |
Tyr1221 |
SPAFDNLyYWDQDPP |
Homo sapiens |
|
| pmid |
sentence |
| 1706616 |
However, each of these peptides contains tyrosines that correspond to major autophosphorylation sites of the epidermal growth factor receptor, suggesting that, in addition to y1023 and y1248, y1139 and y1222 also serve as autophosphorylation sites of her2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124860 |
Tyr1222 |
PAFDNLYyWDQDPPE |
Homo sapiens |
|
| pmid |
sentence |
| 15156151 |
Stimulation of these molecules, however, failed to induce efficient cell migration in the absence of neu/erbb2 phosphorylation at tyr 1201 or tyr 1227 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-21203 |
Tyr1248 |
PTAENPEyLGLDVPV |
Homo sapiens |
|
| pmid |
sentence |
| 1706616 |
However, each of these peptides contains tyrosines that correspond to major autophosphorylation sites of the epidermal growth factor receptor, suggesting that, in addition to y1023 and y1248, y1139 and y1222 also serve as autophosphorylation sites of her2. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| Pathways: | Colorectal Carcinoma |
| + |
PTPN12 | down-regulates activity
dephosphorylation
|
ERBB2 |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277038 |
Tyr1196 |
GAVENPEyLTPQGGA |
Homo sapiens |
|
| pmid |
sentence |
| 29330094 |
In MDA-MB-231 cells, a human triple negative breast cancer cell line, phosphorylation of PTPN12 on Ser 19 was increased in response to cyclin dependent kinase 2 (CDK2), and this impaired PTPN12 's ability to dephosphorylate HER2 on Y1196.|PTPN12 negatively regulates Her2, by dephosphorylation on Tyr 1196 on Her2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
EGFR |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278474 |
Tyr1197 |
STAENAEyLRVAPQS |
Homo sapiens |
|
| pmid |
sentence |
| 23027125 |
HER2 stabilizes EGFR and itself by altering autophosphorylation patterns in a manner that overcomes regulatory mechanisms and promotes proliferative and transformation signaling.|While blocking autophosphorylation on the c-Cbl and the Grb2 binding sites, HER2 promotes EGFR phosphorylation on Y1173 and its own phosphorylation on Y1248 and Y1221/1222 ( xref ). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP3 | down-regulates activity
dephosphorylation
|
ERBB2 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248534 |
Tyr1221 |
SPAFDNLyYWDQDPP |
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 21262974 |
Expression of VHR inhibited the activation of phospholipase Cγ and protein kinase C, both downstream effectors of Tyr-992 phosphorylation of EGFR. | We found that VHR decreased ErbB2 phosphorylation in vitro and in a cellular context, and the dephosphorylation of ErbB2 was more evident at Tyr-877 and Tyr-1221 than those at Tyr-1139 and Tyr-1248 (supplemental Fig. S1). Our data indicated that VHR was a cellular PTP against EGFR and ErbB2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248533 |
Tyr877 |
LDIDETEyHADGGKV |
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 21262974 |
Expression of VHR inhibited the activation of phospholipase Cγ and protein kinase C, both downstream effectors of Tyr-992 phosphorylation of EGFR. | We found that VHR decreased ErbB2 phosphorylation in vitro and in a cellular context, and the dephosphorylation of ErbB2 was more evident at Tyr-877 and Tyr-1221 than those at Tyr-1139 and Tyr-1248 (supplemental Fig. S1). Our data indicated that VHR was a cellular PTP against EGFR and ErbB2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRG | up-regulates activity
dephosphorylation
|
ERBB2 |
0.29 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254701 |
Tyr1248 |
PTAENPEyLGLDVPV |
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 |
| + |
PTPRO | down-regulates quantity by destabilization
dephosphorylation
|
ERBB2 |
0.412 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276979 |
Tyr1248 |
PTAENPEyLGLDVPV |
Homo sapiens |
|
| pmid |
sentence |
| 27345410 |
In this study, our co-immunoprecipitation experiment along with the results derived from in vivo , cultured cells and clinical specimen confirm that PTPRO dephosphorylates ERBB2 at Y1248.|PTPRO overexpression remarkably accelerated degradation of ERBB2 (XREF_FIG). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGFR | up-regulates activity
phosphorylation
|
ERBB2 |
0.598 |
| 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 |
| + |
ERBB2 | up-regulates
phosphorylation
|
DOCK7 |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178348 |
Tyr1257 |
METVPQLyDFTETHN |
Homo sapiens |
|
| pmid |
sentence |
| 18426980 |
We show that the nrg1 receptor erbb2 directly binds and activates dock7 by phosphorylating tyr-1118. thus, dock7 functions as an intracellular substrate for erbb2 to promote schwann cell migration. This provides an unanticipated mechanism through which ligand-dependent tyrosine phosphorylation can trigger the activation of rho gtpase-gefs of the dock180 family. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | down-regulates
phosphorylation
|
CDK1 |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88671 |
Tyr15 |
EKIGEGTyGVVYKGR |
Homo sapiens |
|
| pmid |
sentence |
| 12049736 |
Phosphorylation on tyrosine-15 of p34(cdc2) by erbb2 inhibits p34(cdc2) activation and is involved in resistance to taxol-induced apoptosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | down-regulates quantity by destabilization
phosphorylation
|
BBC3 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276472 |
Tyr152 |
ADDLNAQyERRRQEE |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24236056 |
HER2 phosphorylates and destabilizes pro-apoptotic PUMA. Using an intracellular assay, we found PUMA to be phosphorylated in breast cancer cells with activated HER2. Via cell-free HER2 kinase assay, we observed that PUMA was directly phosphorylated by HER2. Activation of HER2 decreased PUMA protein half-life. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276474 |
Tyr172 |
PSPWRVLyNLIMGLL |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24236056 |
HER2 phosphorylates and destabilizes pro-apoptotic PUMA. Using an intracellular assay, we found PUMA to be phosphorylated in breast cancer cells with activated HER2. Via cell-free HER2 kinase assay, we observed that PUMA was directly phosphorylated by HER2. Activation of HER2 decreased PUMA protein half-life. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276473 |
Tyr58 |
PTLLPAAyLCAPTAP |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24236056 |
HER2 phosphorylates and destabilizes pro-apoptotic PUMA. Using an intracellular assay, we found PUMA to be phosphorylated in breast cancer cells with activated HER2. Via cell-free HER2 kinase assay, we observed that PUMA was directly phosphorylated by HER2. Activation of HER2 decreased PUMA protein half-life. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
PTK2 |
0.645 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278475 |
Tyr397 |
SVSETDDyAEIIDEE |
Homo sapiens |
|
| pmid |
sentence |
| 27638858 |
HER2, EGFR, and additional RTKs directly phosphorylate FAK FERM at Y397.|To further confirm the mechanism of direct FAK activation by HER2, we performed a series of GST pull-down assays with purified recombinant proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | down-regulates activity
phosphorylation
|
CTNNB1 |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279041 |
Tyr654 |
RNEGVATyAAAVLFR |
Homo sapiens |
|
| pmid |
sentence |
| 23576562 |
Second, ErbB2 phosphorylates \u03b2-catenin at Tyr 654, leading to dissociation of the E-cadherin-\u03b2-catenin membrane complex and increased signaling to Wnt target genes such as cyclin D1 ( ). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Colorectal Carcinoma |
| + |
LRIG1 | down-regulates
ubiquitination
|
ERBB2 |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139948 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16123311 |
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. 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 |
| + |
ERBB2 | up-regulates quantity by expression 
transcriptional regulation
|
MSI1 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165195 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20443831 |
We investigated the possibilities that erbb2 may regulate downstream mediators of notch1 signaling to induce musashi1 (which enhances notch1 signaling). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AXL | down-regulates activity
phosphorylation
|
ERBB2 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280193 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20818175 |
Blockade of Axl function abrogated phosphorylation of ERBB2 (Her-2 and neu) at the Tyr877 residue, indicative of receptor crosstalk.|We have demonstrated that either pharmacological or genetic inhibition of Axl function abrogates phosphorylation of ERBB2 at the critical Tyr877 residue and sensitizes OE33 cells to lapatinib in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN9 | down-regulates activity
dephosphorylation
|
ERBB2 |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277170 |
|
|
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 |
| + |
lapatinib | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193627 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177081 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 22056878 |
In estrogen-receptor-negative cellular models showing coamplification of erbb2 and rara, simultaneous targeting of the corresponding gene products with combinations of lapatinib and atra causes synergistic growth inhibition, cyto-differentiation and apoptosis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CUDC-101 | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191148 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
2-methoxy-N-[3-[4-[3-methyl-4-[(6-methyl-3-pyridinyl)oxy]anilino]-6-quinazolinyl]prop-2-enyl]acetamide | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191103 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | up-regulates activity
phosphorylation
|
ERBB2 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279155 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26509276 |
Since Tyr-654 is the ERBB2 phosphorylation site on beta-catenin, this result is consistent with our hypothesis that CDK5 activates ERBB2 , which in turn phosphorylates beta-catenin on Tyr-654, leading to a shift of beta-catenin away from the adherens junction and into the nucleus where it can serve as a transcriptional co-activator.|Taken together with the results of our kinase analysis, these observations suggest that CDK5 phosphorylation of both ERBB2 and ERBB3 and AR could drive a feedback loop, in which ERBB2 and ERBB3 promotes beta-catenin transcriptional activity that then contributes to higher expression of ERBB3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | down-regulates quantity by repression 
deacetylation
|
hsa-miR-139-5p |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277933 |
|
|
Homo sapiens |
SGC-7901 Cell |
| pmid |
sentence |
| 21925125 |
HER2 stabilizes CD44 and activates MTA1/HDAC2 signaling, epigenetically silencing miR-139, leading to CXCR4 upregulation, promoting cancer cell invasion and metastasis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
canertinib | down-regulates activity
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258093 |
|
|
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 |
| + |
ERBB2 | up-regulates quantity by expression
transcriptional regulation
|
NOTCH3 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174747 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 21743488 |
We demonstrate that her2 overexpression in this cellular model of dcis drives transcriptional upregulation of multiple components of the notch survival pathway. Importantly, luminal filling required upregulation of a signaling pathway comprising notch3, its cleaved intracellular domain and the transcriptional regulator hes1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DTX1 | up-regulates quantity by expression
transcriptional regulation
|
ERBB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145319 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16554461 |
Notch1-induced erbb2 expression in cerebellar astroglia occurs via dtx1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
6-{4-[(4-ethylpiperazin-1-yl)methyl]phenyl}-N-[(1R)-1-phenylethyl]-7H-pyrrolo[2,3-d]pyrimidin-4-amine | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189347 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
MBD4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279408 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22964581 |
Importantly, we found that overexpression of HER2 alone is sufficient to induce MED1 phosphorylation at Thr (1032), a key site that is known to be critical for its functions, whereas blockage of HER2 or its downstream MAP kinase diminishes its phosphor ylation levels in these cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
sapitinib | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163730 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190152 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
afatinib | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189359 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196621 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 22418700 |
Afatinib is an oral, erbb family blocker, which covalently binds and irreversibly blocks all kinase-competent erbb family members. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
VARLITINIB | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189903 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
873837-23-1 | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190470 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRIG3 | up-regulates
|
ERBB2 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202180 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23723069 |
Lrig3 opposes lrig1 negative regulatory activity and stabilizes erbb receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CUDC-101 | down-regulates activity
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262255 |
|
|
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 |
| + |
ERBB2 | down-regulates activity
phosphorylation
|
BBC3 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278224 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24236056 |
These results show for the first time that PUMA can be phosphorylated at tyrosine residues directly by HER2.|Together, our results demonstrate, for the first time, that PUMA can be tyrosine phosphorylated and that HER2-mediated phosphorylation destabilizes PUMA protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
canertinib | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191012 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STUB1 | down-regulates quantity by destabilization
ubiquitination, polyubiquitination
|
ERBB2 |
0.619 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278645 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17239458 |
The ErbB2 kinase domain is required for GA-induced and CHIP-dependent ErbB2 ubiquitination and degradation . |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272586 |
|
|
in vitro |
|
| pmid |
sentence |
| 12239347 |
We now show that the chaperone-binding ubiquitin ligase CHIP efficiently ubiquitinates and down-regulates ErbB2. CHIP expression shortens the half-life of both nascent and mature ErbB2 protein. In vitro ubiquitination assay shows that CHIP serves as a ubiquitin ligase for ErbB2, and both exogenously expressed and endogenous CHIP coprecipitate with the kinase. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, In Vitro |
| + |
XL-647 | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207860 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197962 |
|
|
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). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CBL | down-regulates quantity by destabilization
ubiquitination
|
ERBB2 |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-30794 |
|
|
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 |
| + |
ERBB2 | up-regulates quantity by expression
transcriptional regulation
|
CXCL8 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281486 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24041156 |
Direct activation or auto-activation of HER2 can increase IL-8 expression which can further activate CXCR1/2 signaling via a paracrine or autocrine route or both. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
lapatinib | down-regulates activity
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258131 |
|
|
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 |
| + |
AREG | up-regulates
phosphorylation
|
ERBB2 |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-31199 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 7679104 |
Amphiregulin induces tyrosine phosphorylation of the epidermal growth factor receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
dacomitinib | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205939 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200905 |
|
|
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 |
| + |
Arry-380 | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-189882 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates
binding
|
PLCG1 |
0.64 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-20815 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1676673 |
Activated egfr binds the sh2 domain of phospholipase c-gamma (plc-gamma), activating plc-gamma-mediated downstream signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
neratinib | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194631 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202015 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 23632474 |
Ineratinib is a potent irreversible pan-erbb tyrosine kinase inhibitor that has demonstrated antitumour activity and an acceptable safety profile in patients with human epidermal growth factor receptor (her)-2-positive breast cancer and other solid tumours. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates
binding
|
ERBB3 |
0.574 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99569 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12648465 |
Although ErbB-2 binds no known ligand, when recruited into heterodimers it increases ligand binding affinity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43841 |
|
|
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: |
2 |
Organism: |
Homo Sapiens |
| + |
ado-trastuzumab emtansine | down-regulates activity
binding
|
ERBB2 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259882 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19010901 |
The anatomy of an antibody–cytotoxic drug conjugate can be divided into three general components: the antibody, the linker, and the cytotoxic drug. The efficacy of any such conjugate is dictated in part by the differential expression of the target antigen in tumor versus normal tissue. HER2 is a clinically validated target for the treatment of breast cancer. Trastuzumab and, more recently, lapatinib are approved for clinical use in women whose breast cancer overexpresses HER2. a trastuzumab conjugate, which simply uses HER2 as an address for the delivery of a potent cytotoxic agent, may offer promise as an effective therapeutic modality. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates
binding
|
EGFR |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
| + |
ERRFI1 | down-regulates activity
binding
|
ERBB2 |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252077 |
|
|
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 |
| + |
ERBB2 | up-regulates
relocalization
|
SHC3 |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146855 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16729043 |
Erbb3 is characterized by a large number of binding sites for phosphatidylinositol-3-kinase (pi3k), while erbb2 has only few interaction partners with shc as the most frequent one. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
neratinib | down-regulates activity
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258255 |
|
|
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 |
| + |
ERBB2 | up-regulates
relocalization
|
GRB2 |
0.847 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121968 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14967450 |
All erbb ligands and receptors couple to activation of the ras-mapk pathway, either directly through sh2 domain-mediated recruitment of grb-2 or indirectly through ptb domain-mediated binding of the shc adaptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Colorectal Carcinoma |
| + |
ERBB2 | up-regulates
binding
|
SHC1 |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65579 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10085134 |
Shc interacts with and is an excellent substrate for erbb2 and appears to play an important role in mitogenic signaling through this receptor tyrosine kinase |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NRG1 | up-regulates
binding
|
ERBB2 |
0.791 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-26875 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 7514177 |
Direct interaction between heregulin and the two proteins was demonstrated by chemical cross-linking experiments using 125i-heregulin followed by immunoprecipitation with antibodies specific for erbb2 or erbb3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
afatinib | down-regulates activity
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258066 |
|
|
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 |
| + |
ERBB2 | up-regulates
binding
|
ERBB4 |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43844 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8816440 |
Most breast, skin, lung, ovary, and gastrointestinal tract tumors express erbb-4, and heterodimerization of this receptor with erbb-2, may be involved in some cancer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
9-(1-Methyl-4-pyrazolyl)-1-[1-(1-oxoprop-2-enyl)-2,3-dihydroindol-6-yl]-2-benzo[h][1,6]naphthyridinone | down-regulates activity
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262233 |
|
|
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 |
| + |
AV412 | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190053 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOTCH1 | up-regulates quantity by expression
transcriptional regulation
|
ERBB2 |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145322 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16554461 |
Notch1 activation by neuronal contact induces the glial expression of the brain lipid binding protein (blbp) and erbb2 genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN13 | down-regulates activity
dephosphorylation
|
ERBB2 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277087 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19734941 |
Since a previous report showed PTPN13 may dephosphorylate ErbB2 directly, we also examined levels of phospho-ErbB2 (tyr 1248), and we also observed a small effect in the presence of wild-type PTPN13 (XREF_FIG).|The fact that both ErbB2 and H-RasV12 were potentiated by PTPN13 loss and PTPN13 inhibited MAP kinase signaling downstream of multiple oncogenes (ErbB2, EGFR, H-RasV12), suggest that the phosphatase target that inhibits MAP kinase signaling may not only be limited to ErbB2 tyrosine 1248. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
FASN |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278399 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27692180 |
Conversely, HER2 directly phosphorylates and activates FASN, while it also promotes FASN gene expression ( xref ; xref ).|Conversely, HER2 directly phosphorylates and activates FASN, while it also promotes FASN gene expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
ERBB2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279432 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26114632 |
In addition, the c-Src inhibitor 4-(4\u2019-phenoxyanilino)-6,7-dimethoxyquinazoline prevented SP-induced activation of HER2.|On the other hand, c-Src directly phosphorylates the cytoplasmic tails of both EGFR and HER2, allowing the binding of scaffold proteins that will further activate signal transduction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADAM10 | up-regulates activity
cleavage
|
ERBB2 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259845 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26284334 |
The ADAM proteases are best known for their role in shedding the extracellular domain of transmembrane proteins. Among the transmembrane proteins shed by ADAM10 are notch, HER2, E-cadherin, CD44, L1 and the EGFR ligands, EGF and betacellulin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
ErbB receptor family |
0.612 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269875 |
|
|
in vitro |
|
| pmid |
sentence |
| 1706616 |
 Y1023 and Y1248, Y1139 and Y1222 also serve as autophosphorylation sites of HER2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
ERBB3 |
0.574 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278200 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23912457 |
HER2 forms heterodimers with HER3 and thereby phosphorylates and activates HER3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGFR | up-regulates
binding
|
ERBB2 |
0.598 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| 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 |
| + |
JAK2 | up-regulates activity
phosphorylation
|
ERBB2 |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279197 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10938266 |
Our results indicate that autocrine secretion of PRL stimulates tyrosine phosphorylation of ErbB-2 by Jak2, provides docking sites for Grb2 and stimulates Ras-MAP kinase cascade, thereby causing unrestricted cellular proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Mubritinib | down-regulates
chemical inhibition
|
ERBB2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194581 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates activity
phosphorylation
|
ABL1 |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279407 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19275932 |
In this study, we show that Abl kinase SH2 domains bind directly to Her-2, and like PDGFR-beta, Her-2 directly phosphorylates c-Abl. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
trastuzumab | down-regulates activity
binding
|
ERBB2 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259904 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29017563 |
HER2+ breast cancer is associated with poor prognosis and high mortality rates, but the development of HER2-targeted therapies, such as originator trastuzumab (Herceptin®), has substantially improved patient survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates
phosphorylation
|
ESR1 |
0.588 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124962 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15173068 |
The results presented here show for the first time that er redistribution to the cytoplasm and its interaction with her2 are important downstream effects of her2 overexpression, that erk1/2 is important for er cytoplasmic localization, and that subcellular localization of er may play a mechanistic role in determining the responsiveness of breast cancer cells to tamoxifen. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
pertuzumab | down-regulates activity
binding
|
ERBB2 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259900 |
|
|
Homo sapiens |
Carcinoma Cell |
| pmid |
sentence |
| 15093539 |
Pertuzumab binds to ErbB2 near the center of domain II, sterically blocking a binding pocket necessary for receptor dimerization and signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGF | up-regulates
binding
|
ERBB2 |
0.793 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106497 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11279155 |
To better understand the role of the egfr tyrosine kinase, we analyzed signaling by a kinase-inactive egfr (k721m) in erbb-devoid 32d cells. K721m alone exhibited no detectable signaling capacity, whereas coexpression of k721m with erbb2, but not erbb3 or erbb4, resulted in egf-dependent mitogen-activated protein kinase (mapk) activation. The kinase activity, but not tyrosine phosphorylation, of erbb2 was required for egf-induced mapk activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRIG1 | down-regulates
|
ERBB2 |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202143 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23723069 |
Lrig1 is a negative regulator of oncogenic receptor tyrosine kinases, including erbb and met receptors, and promotes receptor degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
ERBB2
- 
- 