ERBB2/HER2 is an ERBB-family plasma-membrane receptor tyrosine kinase that acts as a preferred signaling partner for other ligand-bound ERBB receptors. It lacks a known soluble ligand of its own but forms active homodimers and heterodimers with EGFR, ERBB3, and ERBB4, trans-autophosphorylates receptor tyrosines, and recruits adaptor and effector proteins that activate MAPK and PI3K-AKT signaling. ERBB2 also has nuclear signaling roles and is frequently amplified or mutated in cancers.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001042 RNA polymerase I core binding | IDA PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | KEEP AS NON CORE | Summary: Nuclear ERBB2 physically associates with RNA polymerase I complexes. Reason: RNA polymerase I core binding is supported for nuclear ERBB2, but it is a noncanonical nuclear activity rather than the core plasma-membrane receptor kinase function. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0002116 semaphorin receptor complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB2 can act with Plexin-B1 in a SEMA4D-responsive receptor complex. Reason: The semaphorin/Plexin-B1 receptor complex is a supported ERBB2 signaling context, but it is a specialized output compared with canonical ERBB-family dimer signaling. |
| GO:0002116 semaphorin receptor complex | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ERBB2 can act with Plexin-B1 in a SEMA4D-responsive receptor complex. Reason: The semaphorin/Plexin-B1 receptor complex is a supported ERBB2 signaling context, but it is a specialized output compared with canonical ERBB-family dimer signaling. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | ACCEPT | Summary: The ERBB2 cytoplasmic domain is a protein kinase domain. Reason: This broad kinase-activity inference is consistent with ERBB2 being a catalytically active receptor tyrosine kinase. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:21454582 Structural analysis of the mechanism of inhibition and allos... | ACCEPT | Summary: ERBB2 catalyzes protein tyrosine phosphorylation after receptor dimerization. Reason: Protein tyrosine kinase activity is the defining enzymatic activity of activated ERBB2 homodimers and heterodimers. Supporting Evidence: PMID:21454582 Structural analysis of the mechanism of inhibition and allosteric activation of the kinase domain of HER2 protein. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:12000754 Identification of a region within the ErbB2/HER2 intracellul... | ACCEPT | Summary: ERBB2 catalyzes protein tyrosine phosphorylation after receptor dimerization. Reason: Protein tyrosine kinase activity is the defining enzymatic activity of activated ERBB2 homodimers and heterodimers. Supporting Evidence: PMID:12000754 Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | ACCEPT | Summary: ERBB2 catalyzes protein tyrosine phosphorylation after receptor dimerization. Reason: Protein tyrosine kinase activity is the defining enzymatic activity of activated ERBB2 homodimers and heterodimers. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: ERBB2 catalyzes protein tyrosine phosphorylation after receptor dimerization. Reason: Protein tyrosine kinase activity is the defining enzymatic activity of activated ERBB2 homodimers and heterodimers. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-373750 | ACCEPT | Summary: ERBB2 catalyzes protein tyrosine phosphorylation after receptor dimerization. Reason: Protein tyrosine kinase activity is the defining enzymatic activity of activated ERBB2 homodimers and heterodimers. Supporting Evidence: Reactome:R-HSA-373750 SEMA4D interacts with Plexin-B1:ErbB2 |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: ERBB2 is a single-pass receptor tyrosine kinase active at the plasma membrane. Reason: Transmembrane receptor protein tyrosine kinase activity captures the core molecular role of ERBB2 as an activated ERBB-family receptor kinase. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IDA PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a hig... | ACCEPT | Summary: ERBB2 is a single-pass receptor tyrosine kinase active at the plasma membrane. Reason: Transmembrane receptor protein tyrosine kinase activity captures the core molecular role of ERBB2 as an activated ERBB-family receptor kinase. Supporting Evidence: PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: ERBB2 is a single-pass receptor tyrosine kinase active at the plasma membrane. Reason: Transmembrane receptor protein tyrosine kinase activity captures the core molecular role of ERBB2 as an activated ERBB-family receptor kinase. |
| GO:0004888 transmembrane signaling receptor activity | IDA PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a hig... | ACCEPT | Summary: ERBB2 acts as a transmembrane signaling receptor within ERBB-family dimers. Reason: Although ERBB2 is an orphan receptor that requires dimer partners for ligand-regulated signaling, it is a transmembrane signaling receptor in those complexes. Supporting Evidence: PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. |
| GO:0005102 signaling receptor binding | IPI PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | MODIFY | Summary: The generic signaling-receptor-binding row reflects ERBB2 binding to ERBB3. Reason: GO:0005102 is less informative than the ERBB3-specific function supported by the same HER2/HER3 heterodimerization evidence. Proposed replacements: ErbB-3 class receptor binding Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. |
| GO:0005515 protein binding | IPI PMID:10805725 Class II phosphoinositide 3-kinases are downstream targets o... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:10805725 Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors. |
| GO:0005515 protein binding | IPI PMID:11940572 ErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent ma... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:11940572 ErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent manner. |
| GO:0005515 protein binding | IPI PMID:11940572 ErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent ma... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:11940572 ErbB-2 activates Stat3 alpha in a Src- and JAK2-dependent manner. |
| GO:0005515 protein binding | IPI PMID:12061724 Assignment of backbone 1H, 13C, and 15N resonances of human ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:12061724 Assignment of backbone 1H, 13C, and 15N resonances of human Grb7-SH2 domain in complex with a phosphorylated peptide ligand. |
| GO:0005515 protein binding | IPI PMID:12122014 Csk homologous kinase (CHK) and ErbB-2 interactions are dire... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:12122014 Csk homologous kinase (CHK) and ErbB-2 interactions are directly coupled with CHK negative growth regulatory function in breast cancer. |
| GO:0005515 protein binding | IPI PMID:12975581 Solution structure of the human Grb7-SH2 domain/erbB2 peptid... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:12975581 Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2. |
| GO:0005515 protein binding | IPI PMID:15282549 LRIG1 restricts growth factor signaling by enhancing recepto... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:15282549 LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation. |
| GO:0005515 protein binding | IPI PMID:15345710 The leucine-rich repeat protein LRIG1 is a negative regulato... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:15345710 The leucine-rich repeat protein LRIG1 is a negative regulator of ErbB family receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:15520177 Tid1, the human homologue of a Drosophila tumor suppressor, ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:15520177 Tid1, the human homologue of a Drosophila tumor suppressor, reduces the malignant activity of ErbB-2 in carcinoma cells. |
| GO:0005515 protein binding | IPI PMID:15520177 Tid1, the human homologue of a Drosophila tumor suppressor, ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:15520177 Tid1, the human homologue of a Drosophila tumor suppressor, reduces the malignant activity of ErbB-2 in carcinoma cells. |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:15657067 Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. |
| GO:0005515 protein binding | IPI PMID:15899872 Transforming growth factor {beta} (TGF-{beta})-Smad target g... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:15899872 Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry o... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. |
| GO:0005515 protein binding | IPI PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry o... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. |
| GO:0005515 protein binding | IPI PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry o... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. |
| GO:0005515 protein binding | IPI PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry o... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. |
| GO:0005515 protein binding | IPI PMID:16516204 Activation of ErbB2 by 2-methyl-1,4-naphthoquinone (menadion... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16516204 Activation of ErbB2 by 2-methyl-1,4-naphthoquinone (menadione) in human keratinocytes: role of EGFR and protein tyrosine phosphatases. |
| GO:0005515 protein binding | IPI PMID:16767099 Altered neuregulin 1-erbB4 signaling contributes to NMDA rec... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16767099 Altered neuregulin 1-erbB4 signaling contributes to NMDA receptor hypofunction in schizophrenia. |
| GO:0005515 protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16843263 HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. |
| GO:0005515 protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16843263 HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. |
| GO:0005515 protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16843263 HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. |
| GO:0005515 protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:16843263 HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. |
| GO:0005515 protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:17148612 A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions. |
| GO:0005515 protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:17148612 A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions. |
| GO:0005515 protein binding | IPI PMID:17426253 Growth stimulation of non-small cell lung cancer cell lines ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:17426253 Growth stimulation of non-small cell lung cancer cell lines by antibody against epidermal growth factor receptor promoting formation of ErbB2/ErbB3 heterodimers. |
| GO:0005515 protein binding | IPI PMID:18719096 Brk is coamplified with ErbB2 to promote proliferation in br... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:18719096 Brk is coamplified with ErbB2 to promote proliferation in breast cancer. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19372587 ErbB2-mediated Src and signal transducer and activator of tr... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19372587 ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. |
| GO:0005515 protein binding | IPI PMID:19372587 ErbB2-mediated Src and signal transducer and activator of tr... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19372587 ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. |
| GO:0005515 protein binding | IPI PMID:19411071 Ligand-independent HER2/HER3/PI3K complex is disrupted by tr... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19411071 Ligand-independent HER2/HER3/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941. |
| GO:0005515 protein binding | IPI PMID:19650109 Flow cytometric in situ proximity ligation analyses of prote... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19650109 Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family. |
| GO:0005515 protein binding | IPI PMID:19933325 Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubi... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:19933325 Regulation of Hsp90 client proteins by a Cullin5-RING E3 ubiquitin ligase. |
| GO:0005515 protein binding | IPI PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migr... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migration. |
| GO:0005515 protein binding | IPI PMID:20227043 An activated ErbB3/NRG1 autocrine loop supports in vivo prol... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:20227043 An activated ErbB3/NRG1 autocrine loop supports in vivo proliferation in ovarian cancer cells. |
| GO:0005515 protein binding | IPI PMID:20558745 Secreted heat shock protein 90alpha induces colorectal cance... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:20558745 Secreted heat shock protein 90alpha induces colorectal cancer cell invasion through CD91/LRP-1 and NF-kappaB-mediated integrin alphaV expression. |
| GO:0005515 protein binding | IPI PMID:20650008 Degradation of HER2/neu by ANT2 shRNA suppresses migration a... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:20650008 Degradation of HER2/neu by ANT2 shRNA suppresses migration and invasiveness of breast cancer cells. |
| GO:0005515 protein binding | IPI PMID:20700126 In situ quantification of HER2-protein tyrosine kinase 6 (PT... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:20700126 In situ quantification of HER2-protein tyrosine kinase 6 (PTK6) protein-protein complexes in paraffin sections from breast cancer tissues. |
| GO:0005515 protein binding | IPI PMID:20876300 Progesterone receptor induces ErbB-2 nuclear translocation t... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:20876300 Progesterone receptor induces ErbB-2 nuclear translocation to promote breast cancer growth via a novel transcriptional effect: ErbB-2 function as a coactivator of Stat3. |
| GO:0005515 protein binding | IPI PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab tre... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab treatment of breast cancer cells via Jak2-mediated Src activation and PTEN inactivation. |
| GO:0005515 protein binding | IPI PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab tre... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab treatment of breast cancer cells via Jak2-mediated Src activation and PTEN inactivation. |
| GO:0005515 protein binding | IPI PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab tre... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21075308 Recombinant human erythropoietin antagonizes trastuzumab treatment of breast cancer cells via Jak2-mediated Src activation and PTEN inactivation. |
| GO:0005515 protein binding | IPI PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedbac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer. |
| GO:0005515 protein binding | IPI PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedbac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer. |
| GO:0005515 protein binding | IPI PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedbac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer. |
| GO:0005515 protein binding | IPI PMID:21255571 The tumor suppressor RECK interferes with HER-2/Neu dimeriza... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21255571 The tumor suppressor RECK interferes with HER-2/Neu dimerization and attenuates its oncogenic signaling. |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquired ERK dependency in HER2-overexpressing breast cancer. |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquired ERK dependency in HER2-overexpressing breast cancer. |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquired ERK dependency in HER2-overexpressing breast cancer. |
| GO:0005515 protein binding | IPI PMID:21376233 Activation of multiple proto-oncogenic tyrosine kinases in b... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21376233 Activation of multiple proto-oncogenic tyrosine kinases in breast cancer via loss of the PTPN12 phosphatase. |
| GO:0005515 protein binding | IPI PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0005515 protein binding | IPI PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0005515 protein binding | IPI PMID:21724847 IQGAP1 protein binds human epidermal growth factor receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21724847 IQGAP1 protein binds human epidermal growth factor receptor 2 (HER2) and modulates trastuzumab resistance. |
| GO:0005515 protein binding | IPI PMID:21840311 MEMO associated with an ErbB2 receptor phosphopeptide reveal... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:21840311 MEMO associated with an ErbB2 receptor phosphopeptide reveals a new phosphotyrosine motif. |
| GO:0005515 protein binding | IPI PMID:22279592 ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex reg... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:22279592 ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex regulates MAP kinase signaling in human cancers. |
| GO:0005515 protein binding | IPI PMID:22589551 The atypical histone macroH2A1.2 interacts with HER-2 protei... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:22589551 The atypical histone macroH2A1.2 interacts with HER-2 protein in cancer cells. |
| GO:0005515 protein binding | IPI PMID:22589551 The atypical histone macroH2A1.2 interacts with HER-2 protei... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:22589551 The atypical histone macroH2A1.2 interacts with HER-2 protein in cancer cells. |
| GO:0005515 protein binding | IPI PMID:22733765 Functional isolation of activated and unilaterally phosphory... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:22733765 Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling. |
| GO:0005515 protein binding | IPI PMID:22806884 Spontaneous and pronase-induced HER2 truncation increases th... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:22806884 Spontaneous and pronase-induced HER2 truncation increases the trastuzumab binding capacity of breast cancer tissues and cell lines. |
| GO:0005515 protein binding | IPI PMID:22939624 Quantitative analysis of HSP90-client interactions reveals p... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:22939624 Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. |
| GO:0005515 protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23436906 Parallel visualization of multiple protein complexes in individual cells in tumor tissue. |
| GO:0005515 protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23436906 Parallel visualization of multiple protein complexes in individual cells in tumor tissue. |
| GO:0005515 protein binding | IPI PMID:23680147 Oncogenic ERBB3 mutations in human cancers. | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23680147 Oncogenic ERBB3 mutations in human cancers. |
| GO:0005515 protein binding | IPI PMID:23688700 Design, synthesis and characterization of peptidomimetic con... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23688700 Design, synthesis and characterization of peptidomimetic conjugate of BODIPY targeting HER2 protein extracellular domain. |
| GO:0005515 protein binding | IPI PMID:23723069 Leucine-rich repeat and immunoglobulin domain-containing pro... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23723069 Leucine-rich repeat and immunoglobulin domain-containing protein-1 (Lrig1) negative regulatory action toward ErbB receptor tyrosine kinases is opposed by leucine-rich repeat and immunoglobulin domain-containing protein 3 (Lrig3). |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal growth factor receptors in lung adenocarcinoma cells. |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal growth factor receptors in lung adenocarcinoma cells. |
| GO:0005515 protein binding | IPI PMID:23995768 Paralog-selective Hsp90 inhibitors define tumor-specific reg... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23995768 Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. |
| GO:0005515 protein binding | IPI PMID:23995768 Paralog-selective Hsp90 inhibitors define tumor-specific reg... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:23995768 Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24412244 Charting the molecular links between driver and susceptibili... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24412244 Charting the molecular links between driver and susceptibility genes in colorectal cancer. |
| GO:0005515 protein binding | IPI PMID:24557338 Characterisation of HER heterodimers in breast cancer using ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24557338 Characterisation of HER heterodimers in breast cancer using in situ proximity ligation assay. |
| GO:0005515 protein binding | IPI PMID:24557338 Characterisation of HER heterodimers in breast cancer using ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24557338 Characterisation of HER heterodimers in breast cancer using in situ proximity ligation assay. |
| GO:0005515 protein binding | IPI PMID:24557338 Characterisation of HER heterodimers in breast cancer using ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24557338 Characterisation of HER heterodimers in breast cancer using in situ proximity ligation assay. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells. |
| GO:0005515 protein binding | IPI PMID:24815698 Identification of a Src kinase SH3 binding site in the C-ter... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:24815698 Identification of a Src kinase SH3 binding site in the C-terminal domain of the human ErbB2 receptor tyrosine kinase. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25036637 A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25036637 A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25036637 A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25036637 A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. |
| GO:0005515 protein binding | IPI PMID:25081058 The catalytic region and PEST domain of PTPN18 distinctly re... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25081058 The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes. |
| GO:0005515 protein binding | IPI PMID:25081058 The catalytic region and PEST domain of PTPN18 distinctly re... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25081058 The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25241761 Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25241761 Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25241761 Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25241761 Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25241761 Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network. |
| GO:0005515 protein binding | IPI PMID:25326665 Pharmacological targeting of the pseudokinase Her3. | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25326665 Pharmacological targeting of the pseudokinase Her3. |
| GO:0005515 protein binding | IPI PMID:25640309 Systematic identification of molecular links between core an... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:25640309 Systematic identification of molecular links between core and candidate genes in breast cancer. |
| GO:0005515 protein binding | IPI PMID:26517842 Client Proteins and Small Molecule Inhibitors Display Distin... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:26517842 Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants. |
| GO:0005515 protein binding | IPI PMID:26517842 Client Proteins and Small Molecule Inhibitors Display Distin... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:26517842 Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants. |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome. |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome. |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome. |
| GO:0005515 protein binding | IPI PMID:31862538 Neuropeptide bombesin receptor activation stimulates growth ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31862538 Neuropeptide bombesin receptor activation stimulates growth of lung cancer cells through HER3 with a MAPK-dependent mechanism. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35384245 Physical and functional interactome atlas of human receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35512704 Systematic discovery of mutation-directed neo-protein-protein interactions in cancer. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:35512704 Systematic discovery of mutation-directed neo-protein-protein interactions in cancer. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36115835 Quantitative fragmentomics allow affinity mapping of interactomes. |
| GO:0005515 protein binding | IPI PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human c... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:36931259 A central chaperone-like role for 14-3-3 proteins in human cells. |
| GO:0005515 protein binding | IPI PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment-mass spectrometry. |
| GO:0005515 protein binding | IPI PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0005515 protein binding | IPI PMID:7592681 Binding of Neu differentiation factor with the extracellular... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:7592681 Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. |
| GO:0005515 protein binding | IPI PMID:7592681 Binding of Neu differentiation factor with the extracellular... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:7592681 Binding of Neu differentiation factor with the extracellular domain of Her2 and Her3. |
| GO:0005515 protein binding | IPI PMID:9079677 Structural determinants of the interaction between the erbB2... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:9079677 Structural determinants of the interaction between the erbB2 receptor and the Src homology 2 domain of Grb7. |
| GO:0005515 protein binding | IPI PMID:9705354 Tyrosine phosphorylation of c-ErbB-2 is regulated by the cel... | REMOVE | Summary: The evidence reports an ERBB2 physical interactor, but the GO term is only generic protein binding. Reason: GO:0005515 is a catch-all interaction term and should not be retained for ERBB2 unless the row is curated to a receptor-dimerization, SH2-docking, chaperone-binding, or other specific molecular function supported by the experiment. Supporting Evidence: PMID:9705354 Tyrosine phosphorylation of c-ErbB-2 is regulated by the cellular form of prostatic acid phosphatase in human prostate cancer cells. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: ATP binding is required for catalysis by the ERBB2 kinase domain. Reason: ATP binding is mechanistically correct for the kinase domain but less informative than the core tyrosine kinase activity. |
| GO:0005634 nucleus | IDA PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry o... | KEEP AS NON CORE | Summary: ERBB2 can undergo endocytosis-dependent nuclear translocation. Reason: Nuclear localization is experimentally supported for full-length or intracellular ERBB2, but it is a secondary localization relative to the core plasma-membrane receptor pool. Supporting Evidence: PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. |
| GO:0005634 nucleus | IDA PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | KEEP AS NON CORE | Summary: ERBB2 can undergo endocytosis-dependent nuclear translocation. Reason: Nuclear localization is experimentally supported for full-length or intracellular ERBB2, but it is a secondary localization relative to the core plasma-membrane receptor pool. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: ERBB2 can undergo endocytosis-dependent nuclear translocation. Reason: Nuclear localization is experimentally supported for full-length or intracellular ERBB2, but it is a secondary localization relative to the core plasma-membrane receptor pool. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: ERBB2 has been detected in the nucleoplasm in high-throughput imaging. Reason: The nucleoplasm row is compatible with reports of nuclear ERBB2, but it is a less central localization than plasma membrane and endosomal trafficking compartments. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Cytoplasmic ERBB2 reflects internalized receptor and cytoplasmic C-terminal isoforms. Reason: Cytoplasmic localization is plausible for internalized and truncated ERBB2 species, but the canonical receptor is a plasma-membrane protein. |
| GO:0005769 early endosome | EXP PMID:31138794 SORLA regulates endosomal trafficking and oncogenic fitness ... | KEEP AS NON CORE | Summary: ERBB2 traffics through early endosomes after endocytosis. Reason: Early endosomal ERBB2 is part of receptor trafficking and sorting rather than the primary active membrane pool. Supporting Evidence: PMID:31138794 SORLA regulates endosomal trafficking and oncogenic fitness of HER2. |
| GO:0005769 early endosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: ERBB2 traffics through early endosomes after endocytosis. Reason: Early endosomal ERBB2 is part of receptor trafficking and sorting rather than the primary active membrane pool. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Cytosolic signal is a broad localization for internalized or truncated ERBB2 species. Reason: The cytosol annotation is kept as a non-core localization because full-length ERBB2 is membrane anchored. |
| GO:0005886 plasma membrane | EXP PMID:31138794 SORLA regulates endosomal trafficking and oncogenic fitness ... | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: PMID:31138794 SORLA regulates endosomal trafficking and oncogenic fitness of HER2. |
| GO:0005886 plasma membrane | EXP PMID:32381043 SH3BGRL confers innate drug resistance in breast cancer by s... | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: PMID:32381043 SH3BGRL confers innate drug resistance in breast cancer by stabilizing HER2 activation on cell membrane. |
| GO:0005886 plasma membrane | EXP PMID:33497358 Dysregulation of the NRG1/ERBB pathway causes a developmenta... | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: PMID:33497358 Dysregulation of the NRG1/ERBB pathway causes a developmental disorder with gastrointestinal dysmotility in humans. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. |
| GO:0005886 plasma membrane | IDA PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migr... | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migration. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. |
| GO:0005886 plasma membrane | NAS PMID:12000754 Identification of a region within the ErbB2/HER2 intracellul... | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: PMID:12000754 Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1227964 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1227964 ERBB2 homodimerization |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1248694 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1248694 Trans-autophosphorylation of ERBB2 homodimer |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250189 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1250189 Binding of PI3K to ERBB2:p-ERBB3 heterodimer |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250195 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1250195 SHC1 phosphorylation by ERBB2 heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250346 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1250346 Binding of PI3K to p-ERBB2:p-ERBB4 CYT-1 heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250462 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1250462 PIP2 to PIP3 conversion by PI3K bound to phosphorylated heterodimer of ERBB2 and ERBB3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306953 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1306953 GRB7 binds phosphorylated heterodimer of ERBB2 and ERBB3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306957 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1306957 PIP2 to PIP3 conversion by PI3K bound to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306963 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1306963 Binding of GRB2:GAB1 to p-ERBB2:p-EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306965 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1306965 Binding of PI3K to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306969 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1306969 GRB2:SOS1 complex binds phosphorylated ERBB4:ERBB2 heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306972 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1306972 RAS guanyl nucleotide exchange mediated by SOS1 bound to GRB2 in complex with phosphorylated ERBB4:ERBB2 heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306979 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1306979 PIP2 to PIP3 conversion by PI3K bound to phosphorylated heterodimer of ERBB2 and ERBB4 CYT1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1358792 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1358792 RNF41 ubiquitinates activated ERBB3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1358798 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1358798 RNF41 binds neuregulin-activated ERBB3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1918092 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1918092 CHIP (STUB1) mediates ubiquitination of ERBB2 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1918095 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1918095 CUL5 mediates ubiquitination of ERBB2 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963563 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1963563 MATK (CSK homologous kinase) binds phosphorylated ERBB2 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963581 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1963581 Trans-autophosphorylation of p-Y877-ERBB2 heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963582 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1963582 Trans-autophosphorylation of ERBB2 heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963586 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1963586 SRC family kinases phosphorylate ERBB2 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963589 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-1963589 ERBB2 forms heterodimers with ligand-activated ERBB receptors: EGFR, ERBB3 and ERBB4 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-2316434 PI3K phosphorylates PIP2 to PIP3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-2400009 PI3K inhibitors block PI3K catalytic activity |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-373750 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-373750 SEMA4D interacts with Plexin-B1:ErbB2 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-416588 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-416588 Activation of Rho by LARG and PDZ-RhoGEF |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-416594 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-416594 LARG and PDZ-RhoGEF binds to Plexin-B1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672965 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-5672965 RAS GEFs promote RAS nucleotide exchange |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6785636 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-6785636 Phosphorylated ERBB2 heterodimers bind MEMO1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6785648 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-6785648 MEMO1 binds RHOA:GTP:DIAPH1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8847995 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-8847995 Activated ERBB2 binds PTK6 (BRK) |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8848005 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-8848005 ERBB2 promotes PTK6 autophosphorylation |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8863804 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-8863804 PTPN12 dephosphorylates ERBB2 on tyrosine Y1248 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864105 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-8864105 PTPN18 binds ERBB2:EGFR heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864125 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-8864125 PTPN18 dephosphorylates ERBB2 at Y1196, Y1112 and Y1248 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864466 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-8864466 TFAP2A,(TFAP2B,TFAP2C) homo- and heterodimers and YY1 stimulate ERBB2 gene expression |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634390 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9634390 ERBB2 homodimer phosphorylates SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634391 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9634391 SHC1 binds phosphorylated ERBB2 homodimer |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634402 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9634402 Recruitment of GRB2:SOS1 to p-SHC1 in complex with phosphorylated ERBB2 homodimer |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634418 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9634418 RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and ERBB2 homodimer:p-SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9649393 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9649393 ERBB2 KD mutants bind trastuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9652264 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9652264 ERBB2 binds TKIs |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9652277 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9652277 ERBB2 binds trastuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664567 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664567 ERBB2 KD mutants heterodimerize |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664588 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664588 ERBB2 KD mutants trans-autophosphorylate |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664646 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664646 Phosphorylated heterodimers of ERBB2 KD mutants and ERBB3 bind PI3K |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664664 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664664 PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and ERBB3 converts PIP2 to PIP3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664918 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664918 Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:GAB1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664933 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664933 Phosphorylated heterodimers of ERBB2 KD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664940 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664940 PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR converts PIP2 to PIP3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664950 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664950 Phosphorylated heterodimers of ERBB2 KD mutants bind SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664976 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664976 Phosphorylated heterodimers of ERBB2 KD mutants phosphorylate SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664983 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664983 Phosphorylated heterodimers of ERBB2 KD mutants recruit GRB2:SOS1 through SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664991 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9664991 RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665000 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665000 Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:SOS1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665009 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665009 RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665032 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665032 Phosphorylated heterodimers of ERBB2 KD mutants and EGFR phosphorylate PLCG1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665034 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665034 Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind PLCG1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665121 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665121 ERBB2 KD mutants bind TKIs |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665232 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665232 Resistant ERBB2 KD mutants do not bind trastuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665278 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665278 Resistant ERBB2 KD mutants do not bind AEE788 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665280 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665280 ERBB2 KD mutants do not bind osimertinib |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665284 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665284 Resistant ERBB2 KD mutants do not bind lapatinib |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665286 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665286 Resistant ERBB2 KD mutants do not bind neratinib |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665304 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665304 ERBB2 T862A does not bind sapitinib |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665311 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665311 ERBB2 T798M does not bind afatinib |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665315 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665315 ERBB2 T733I does not bind tesevatinib |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665388 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665388 ERBB2 ECD mutants heterodimerize with EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665389 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665389 Heterodimers of ERBB2 ECD mutants and EGFR trans-autophosphorylate |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665404 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665404 RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665405 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665405 ERBB2 ECD mutants bind trastuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665406 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665406 Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665407 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665407 PI3K bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR converts PIP2 to PIP3 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665408 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665408 RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR through GRB2 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665409 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665409 GRB2:SOS1 binds to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665410 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665410 Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind PLCG1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665411 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665411 Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate PLCG1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665412 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665412 ERBB2 ECD mutants bind TKIs |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665413 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665413 Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR recruit GRB2:SOS1 through SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665415 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665415 Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665416 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665416 Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665417 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665417 Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind GRB2:GAB1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665696 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665696 ERBB2 TMD/JMD mutants bind trastuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665697 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665697 ERBB2 TMD/JMD mutants hetrodimerize |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665698 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665698 Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind GRB2:SOS1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665699 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665699 Phosphorylated heterodimers of ERBB2 TMD/JMD mutants recruit GRB2:SOS1 through SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665700 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665700 RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665701 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665701 Phosphorylated ERBB2 TMD/JMD heterodimers bind SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665702 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665702 ERBB2 TMD/JMD mutants bind TKIs |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665703 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665703 ERBB2 TMD/JMD mutants bind pertuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665704 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665704 Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665705 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665705 Phosphorylated heterodimers of ERBB2 TMD/JMD mutants phosphorylate SHC1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665706 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665706 Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind PLCG1 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665707 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665707 RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665708 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665708 ERBB2 TMD/JMD mutants do not bind pertuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665709 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665709 ERBB2 TMD/JMD heterodimers trans-autophosphorylate |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665726 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-HSA-9665726 ERBB2 binds pertuzumab |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1248744 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-NUL-1248744 Shc1 binds phosphorylated ERBB2:EGFR heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1248753 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-NUL-1248753 Shc1 binds phosphorylated ERBB2:ERBB3 heterodimers |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1251923 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-NUL-1251923 Plcg1 binds P-ERBB2:P-EGFR |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1251929 | ACCEPT | Summary: ERBB2 is a type I plasma-membrane receptor and the cited evidence places ERBB2-containing signaling complexes at the plasma membrane. Reason: Plasma membrane localization is the canonical localization for full-length ERBB2; the many Reactome TAS events are redundant event-level supports for the same receptor location but are biologically sound. Supporting Evidence: Reactome:R-NUL-1251929 Plcg1 phosphorylation by P-ERBB2:P-EGFR |
| GO:0006468 protein phosphorylation | TAS PMID:10851066 Interaction between protein tyrosine phosphatase and protein... | MODIFY | Summary: ERBB2 is a receptor tyrosine kinase whose direct reaction is tyrosine phosphorylation. Reason: GO:0006468 is a broad protein-phosphorylation process; the ERBB2 kinase specifically catalyzes peptidyl-tyrosine phosphorylation. Proposed replacements: peptidyl-tyrosine phosphorylation Supporting Evidence: PMID:10851066 Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells. |
| GO:0007165 signal transduction | IDA PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | MODIFY | Summary: The cited ErbB-1/ErbB-2 heterodimer study supports the more specific MAP kinase activation already curated from the same paper. Reason: GO:0007165 is an uninformative ancestor for ERBB2; the same evidence supports positive regulation of MAP kinase activity downstream of ErbB heterodimers. Proposed replacements: positive regulation of MAP kinase activity Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. |
| GO:0007166 cell surface receptor signaling pathway | IDA PMID:9685399 Reciprocal regulation of neu tyrosine kinase activity and ca... | KEEP AS NON CORE | Summary: ERBB2 transduces signals from the cell surface in ERBB-family receptor complexes. Reason: The broad cell-surface receptor signaling term is true but less informative than ERBB2-EGFR, ERBB2-ERBB3, ERBB2-ERBB4, MAPK, or PI3K pathway terms. Supporting Evidence: PMID:9685399 Reciprocal regulation of neu tyrosine kinase activity and caveolin-1 protein expression in vitro and in vivo. Implications for human breast cancer. |
| GO:0007167 enzyme-linked receptor protein signaling pathway | TAS PMID:9590694 Requirement of ErbB2 for signalling by interleukin-6 in pros... | KEEP AS NON CORE | Summary: ERBB2 participates in enzyme-linked receptor signaling. Reason: The term is a very broad ancestor of receptor tyrosine kinase signaling; it is valid but not a precise statement of ERBB2 function. Supporting Evidence: PMID:9590694 Requirement of ErbB2 for signalling by interleukin-6 in prostate carcinoma cells. |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IDA PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a hig... | ACCEPT | Summary: ERBB2 executes receptor tyrosine kinase signaling from ERBB-family dimers. Reason: Cell surface receptor protein tyrosine kinase signaling is central to ERBB2 function, although ERBB-specific child terms are more precise where they are available. Supporting Evidence: PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IDA PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | ACCEPT | Summary: ERBB2 executes receptor tyrosine kinase signaling from ERBB-family dimers. Reason: Cell surface receptor protein tyrosine kinase signaling is central to ERBB2 function, although ERBB-specific child terms are more precise where they are available. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: ERBB2 executes receptor tyrosine kinase signaling from ERBB-family dimers. Reason: Cell surface receptor protein tyrosine kinase signaling is central to ERBB2 function, although ERBB-specific child terms are more precise where they are available. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: ERBB2 participates in EGFR-family signaling as the kinase subunit in EGF-bound EGFR:ERBB2 heterodimers. Reason: The PAINT IBA row is consistent with experimentally curated human and mouse ERBB2-EGFR signaling models. |
| GO:0008283 cell population proliferation | IDA PMID:36949068 IGFBP5 is an ROR1 ligand promoting glioblastoma invasion via... | KEEP AS NON CORE | Summary: ERBB2 kinase activity can drive glioblastoma cell proliferation downstream of ROR1/IGFBP5 signaling. Reason: The proliferation row is a pathway outcome in a tumor signaling context rather than a direct molecular activity of ERBB2. Supporting Evidence: PMID:36949068 IGFBP5 is an ROR1 ligand promoting glioblastoma invasion via ROR1/HER2-CREB signaling axis. |
| GO:0009925 basal plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: ERBB2 family receptors can signal from the basal plasma membrane in polarized epithelial contexts. Reason: Basal plasma membrane localization is a supported specialized membrane subregion and a child of ERBB2 core plasma-membrane localization. |
| GO:0010008 endosome membrane | IDA PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry o... | KEEP AS NON CORE | Summary: Internalized ERBB2 traffics on endosomal membranes. Reason: Endosomal-membrane localization is supported as a route for nuclear entry and receptor sorting, but is secondary to plasma-membrane signaling. Supporting Evidence: PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. |
| GO:0014044 Schwann cell development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB2/Erbb2 signaling has neural and glial developmental roles in mammals. Reason: Schwann cell development is kept as a neural developmental output of ERBB signaling rather than the core biochemical function of the receptor. |
| GO:0015026 coreceptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: ERBB2 can function as a ligand-binding coreceptor in ERBB and Plexin receptor complexes. Reason: Coreceptor activity reflects the key HER2 property of partnering with ligand-bound receptors while contributing the active kinase and allosteric dimer interface. |
| GO:0015026 coreceptor activity | ISS GO_REF:0000024 | ACCEPT | Summary: ERBB2 can function as a ligand-binding coreceptor in ERBB and Plexin receptor complexes. Reason: Coreceptor activity reflects the key HER2 property of partnering with ligand-bound receptors while contributing the active kinase and allosteric dimer interface. |
| GO:0016020 membrane | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: ERBB2 is an integral single-pass membrane receptor. Reason: Generic membrane localization is accurate but less specific than the plasma-membrane and ERBB3:ERBB2 complex annotations. |
| GO:0016020 membrane | NAS PMID:15609325 Identification and validation of novel ERBB2 (HER2, NEU) tar... | KEEP AS NON CORE | Summary: ERBB2 is an integral single-pass membrane receptor. Reason: Generic membrane localization is accurate but less specific than the plasma-membrane and ERBB3:ERBB2 complex annotations. Supporting Evidence: PMID:15609325 Identification and validation of novel ERBB2 (HER2, NEU) targets including genes involved in angiogenesis. |
| GO:0016323 basolateral plasma membrane | IDA PMID:12646923 Segregation of receptor and ligand regulates activation of e... | KEEP AS NON CORE | Summary: ERBB2 localizes to the basolateral plasma membrane in polarized airway epithelia. Reason: Basolateral localization is a real epithelial context that enables heregulin responsiveness after barrier disruption, but it is a specialized form of plasma-membrane localization. Supporting Evidence: PMID:12646923 Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ERBB2 localizes to the basolateral plasma membrane in polarized airway epithelia. Reason: Basolateral localization is a real epithelial context that enables heregulin responsiveness after barrier disruption, but it is a specialized form of plasma-membrane localization. |
| GO:0016324 apical plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB orthology supports an apical plasma-membrane localization row for a receptor subpopulation. Reason: This epithelial polarity row is kept as non-core because the main ERBB2 localization is the plasma membrane without apical restriction. |
| GO:0018108 peptidyl-tyrosine phosphorylation | IDA PMID:12000754 Identification of a region within the ErbB2/HER2 intracellul... | ACCEPT | Summary: ERBB2 activation causes tyrosine phosphorylation of the receptor complex. Reason: Peptidyl-tyrosine phosphorylation is the immediate reaction catalyzed by the activated ERBB2 kinase domain. Supporting Evidence: PMID:12000754 Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. |
| GO:0019838 growth factor binding | IDA PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a hig... | ACCEPT | Summary: ERBB2 contributes to growth-factor binding by ERBB3-containing neuregulin receptor complexes. Reason: The contributes_to annotation is appropriate because ERBB2 increases high-affinity ligand binding by ERBB3 without itself being the direct neuregulin-binding subunit. Supporting Evidence: PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. |
| GO:0030182 neuron differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: ERBB-family signaling contributes to neuronal differentiation outputs. Reason: Neuron differentiation is a downstream developmental phenotype of ERBB signaling, not the core ERBB2 molecular activity. |
| GO:0030307 positive regulation of cell growth | IMP PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | KEEP AS NON CORE | Summary: Nuclear ERBB2 can increase cell growth by stimulating Pol I-dependent rRNA synthesis. Reason: Cell growth is supported in the nuclear ERBB2 context but is downstream of noncanonical transcriptional regulation. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0030971 receptor tyrosine kinase binding | IPI PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | ACCEPT | Summary: ERBB2 binds receptor tyrosine kinase partners in ERBB-family dimers. Reason: Receptor tyrosine kinase binding captures ERBB2 dimerization with ERBB-family receptor partners and is more informative than generic protein binding. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0031410 cytoplasmic vesicle | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: A vesicular ERBB2 pool is compatible with receptor endocytosis and retrograde trafficking. Reason: Cytoplasmic-vesicle localization is a broad trafficking location rather than the primary signaling site of ERBB2. |
| GO:0031594 neuromuscular junction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mammalian ERBB signaling has specialized synaptic contexts. Reason: Neuromuscular-junction localization is retained as a non-core neural/synaptic context inferred from mammalian ERBB orthology. |
| GO:0032587 ruffle membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: ERBB2 can be found on ruffle membranes during receptor-driven cell motility. Reason: Ruffle-membrane localization is a specialized motility-associated plasma-membrane subdomain. |
| GO:0032886 regulation of microtubule-based process | IDA PMID:20937854 ErbB2 receptor controls microtubule capture by recruiting AC... | KEEP AS NON CORE | Summary: ERBB2 signaling regulates microtubule capture through MEMO1/RHOA/DIAPH1/GSK3B/APC/CLASP2/MACF1 signaling. Reason: Microtubule stabilization is a downstream motility output of ERBB2 rather than its core kinase activity. Supporting Evidence: PMID:20937854 ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. |
| GO:0035025 positive regulation of Rho protein signal transduction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB2 participates in SEMA4D/Plexin-B1 signaling that activates RhoA. Reason: Rho activation is a Plexin-B1/PDZRhoGEF/LARG output in a specialized semaphorin context and is not the canonical ERBB2 output. |
| GO:0035025 positive regulation of Rho protein signal transduction | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ERBB2 participates in SEMA4D/Plexin-B1 signaling that activates RhoA. Reason: Rho activation is a Plexin-B1/PDZRhoGEF/LARG output in a specialized semaphorin context and is not the canonical ERBB2 output. |
| GO:0035556 intracellular signal transduction | IDA PMID:19372587 ErbB2-mediated Src and signal transducer and activator of tr... | KEEP AS NON CORE | Summary: ERBB2 activates intracellular signaling through Src, STAT3, PI3K, and MAPK routes. Reason: The broad intracellular signal transduction row is true but less informative than ERBB2-specific downstream pathway terms. Supporting Evidence: PMID:19372587 ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. |
| GO:0038127 ERBB signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: ERBB2 is an ERBB-family receptor that signals through ligand-regulated dimers. Reason: ERBB signaling pathway is an appropriate parent for ERBB2-EGFR, ERBB2-ERBB3, and ERBB2-ERBB4 signaling. |
| GO:0038128 ERBB2 signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: ERBB2 homodimers signal when ERBB2 is overexpressed or oncogenically activated. Reason: ERBB2-specific signaling captures ligand-independent HER2 homodimer signaling as represented by Reactome and cancer biology. |
| GO:0038133 ERBB2-ERBB3 signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: ERBB2 is the catalytically active kinase partner in neuregulin-induced ERBB2:ERBB3 signaling. Reason: ERBB2-ERBB3 signaling is one of the canonical ERBB2 heterodimer pathways. |
| GO:0038134 ERBB2-EGFR signaling pathway | IDA PMID:8702723 The epidermal growth factor receptor couples transforming gr... | ACCEPT | Summary: ERBB2 signals with ligand-activated EGFR in ERBB2-EGFR heterodimers. Reason: ERBB2-EGFR signaling is a canonical route by which EGF-family ligands activate HER2 kinase signaling. Supporting Evidence: PMID:8702723 The epidermal growth factor receptor couples transforming growth factor-alpha, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4. |
| GO:0038134 ERBB2-EGFR signaling pathway | IDA PMID:8702723 The epidermal growth factor receptor couples transforming gr... | ACCEPT | Summary: ERBB2 signals with ligand-activated EGFR in ERBB2-EGFR heterodimers. Reason: ERBB2-EGFR signaling is a canonical route by which EGF-family ligands activate HER2 kinase signaling. Supporting Evidence: PMID:8702723 The epidermal growth factor receptor couples transforming growth factor-alpha, heparin-binding epidermal growth factor-like factor, and amphiregulin to Neu, ErbB-3, and ErbB-4. |
| GO:0038134 ERBB2-EGFR signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: ERBB2 signals with ligand-activated EGFR in ERBB2-EGFR heterodimers. Reason: ERBB2-EGFR signaling is a canonical route by which EGF-family ligands activate HER2 kinase signaling. |
| GO:0038135 ERBB2-ERBB4 signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: ERBB2 signals with ligand-activated ERBB4 in ERBB2-ERBB4 heterodimers. Reason: ERBB2-ERBB4 signaling is a canonical neuregulin/ERBB-family heterodimer route. |
| GO:0038143 ERBB3:ERBB2 complex | IDA PMID:12000754 Identification of a region within the ErbB2/HER2 intracellul... | ACCEPT | Summary: ERBB2 forms receptor complexes with ERBB3. Reason: ERBB3:ERBB2 complex membership is core to HER2 biology because ERBB2 supplies kinase activity to the ERBB3 pseudokinase receptor complex. Supporting Evidence: PMID:12000754 Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. |
| GO:0042060 wound healing | IDA PMID:12646923 Segregation of receptor and ligand regulates activation of e... | KEEP AS NON CORE | Summary: Basolateral ERBB2/ERBB3/ERBB4 activation can promote airway epithelial wound repair. Reason: Wound healing is a context-specific epithelial outcome downstream of heregulin-stimulated ERBB receptors. Supporting Evidence: PMID:12646923 Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. |
| GO:0042127 regulation of cell population proliferation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ERBB2 signaling regulates proliferation downstream of ERBB and tumor signaling pathways. Reason: Cell-proliferation regulation is a major phenotype of ERBB2 activity but still a downstream outcome. |
| GO:0042734 presynaptic membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB orthology supports a presynaptic localization row for neural receptor signaling contexts. Reason: Presynaptic localization is a specialized neural context and not the dominant ERBB2 membrane compartment. |
| GO:0042802 identical protein binding | IPI PMID:12000754 Identification of a region within the ErbB2/HER2 intracellul... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:12000754 Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. |
| GO:0042802 identical protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:16843263 HER2 kinase domain mutation results in constitutive phosphorylation and activation of HER2 and EGFR and resistance to EGFR tyrosine kinase inhibitors. |
| GO:0042802 identical protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:17148612 A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions. |
| GO:0042802 identical protein binding | IPI PMID:19650109 Flow cytometric in situ proximity ligation analyses of prote... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:19650109 Flow cytometric in situ proximity ligation analyses of protein interactions and post-translational modification of the epidermal growth factor receptor family. |
| GO:0042802 identical protein binding | IPI PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedbac... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancer. |
| GO:0042802 identical protein binding | IPI PMID:21255571 The tumor suppressor RECK interferes with HER-2/Neu dimeriza... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:21255571 The tumor suppressor RECK interferes with HER-2/Neu dimerization and attenuates its oncogenic signaling. |
| GO:0042802 identical protein binding | IPI PMID:21480528 Comparative analysis of fluorescence resonance energy transf... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:21480528 Comparative analysis of fluorescence resonance energy transfer (FRET) and proximity ligation assay (PLA). |
| GO:0042802 identical protein binding | IPI PMID:22733765 Functional isolation of activated and unilaterally phosphory... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:22733765 Functional isolation of activated and unilaterally phosphorylated heterodimers of ERBB2 and ERBB3 as scaffolds in ligand-dependent signaling. |
| GO:0042802 identical protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | ACCEPT | Summary: ERBB2 can form ligand-independent homodimers when overexpressed or activated by mutation. Reason: Identical protein binding captures HER2 homodimer formation, a well-established mode of oncogenic ERBB2 signaling. Supporting Evidence: PMID:23436906 Parallel visualization of multiple protein complexes in individual cells in tumor tissue. |
| GO:0043066 negative regulation of apoptotic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: ERBB-family signaling can oppose apoptosis through MAPK and PI3K/AKT outputs. Reason: Negative regulation of apoptosis is a downstream signaling phenotype and is less direct than the receptor kinase and named ERBB pathway terms. |
| GO:0043125 ErbB-3 class receptor binding | IPI PMID:12000754 Identification of a region within the ErbB2/HER2 intracellul... | ACCEPT | Summary: ERBB2 binds ERBB3 to form high-affinity neuregulin receptor complexes. Reason: ErbB-3 class receptor binding is a specific and central ERBB2 molecular function. Supporting Evidence: PMID:12000754 Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association. |
| GO:0043125 ErbB-3 class receptor binding | TAS PMID:9590694 Requirement of ErbB2 for signalling by interleukin-6 in pros... | ACCEPT | Summary: ERBB2 binds ERBB3 to form high-affinity neuregulin receptor complexes. Reason: ErbB-3 class receptor binding is a specific and central ERBB2 molecular function. Supporting Evidence: PMID:9590694 Requirement of ErbB2 for signalling by interleukin-6 in prostate carcinoma cells. |
| GO:0043209 myelin sheath | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB2/Erbb2 is implicated in myelinating-cell signaling in mammals. Reason: Myelin-sheath localization is retained as a specialized neural context inferred from mammalian ERBB signaling. |
| GO:0043235 signaling receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: ERBB2 is part of activated ERBB-family signaling receptor complexes. Reason: Signaling receptor complex membership accurately captures activated ERBB2 homodimers and heterodimers. |
| GO:0043235 signaling receptor complex | IDA PMID:23382219 Structural basis for endosomal trafficking of diverse transm... | ACCEPT | Summary: ERBB2 is part of activated ERBB-family signaling receptor complexes. Reason: Signaling receptor complex membership accurately captures activated ERBB2 homodimers and heterodimers. Supporting Evidence: PMID:23382219 Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. |
| GO:0043235 signaling receptor complex | IDA PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a hig... | ACCEPT | Summary: ERBB2 is part of activated ERBB-family signaling receptor complexes. Reason: Signaling receptor complex membership accurately captures activated ERBB2 homodimers and heterodimers. Supporting Evidence: PMID:7514177 Coexpression of erbB2 and erbB3 proteins reconstitutes a high affinity receptor for heregulin. |
| GO:0043235 signaling receptor complex | TAS PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | ACCEPT | Summary: ERBB2 is part of activated ERBB-family signaling receptor complexes. Reason: Signaling receptor complex membership accurately captures activated ERBB2 homodimers and heterodimers. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0043406 positive regulation of MAP kinase activity | IDA PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | ACCEPT | Summary: ERBB2 signaling activates MAP kinase activity. Reason: Positive regulation of MAP kinase activity is a central downstream output of ligand-activated ERBB2 receptor dimers. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. |
| GO:0043410 positive regulation of MAPK cascade | IBA GO_REF:0000033 | ACCEPT | Summary: ERBB2 receptor dimers positively regulate the MAPK cascade. Reason: MAPK-cascade activation is a canonical output of ERBB2-EGFR, ERBB2-ERBB3, and ERBB2 homodimer signaling. |
| GO:0043410 positive regulation of MAPK cascade | IEA GO_REF:0000117 | ACCEPT | Summary: ERBB2 receptor dimers positively regulate the MAPK cascade. Reason: MAPK-cascade activation is a canonical output of ERBB2-EGFR, ERBB2-ERBB3, and ERBB2 homodimer signaling. |
| GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction | IDA PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | ACCEPT | Summary: ERBB2-ERBB3 and related dimers activate PI3K/AKT signaling. Reason: PI3K/AKT signaling is a canonical pathway downstream of phosphorylated ERBB2-containing receptor dimers. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0045211 postsynaptic membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB orthology supports postsynaptic signaling contexts for this receptor family. Reason: Postsynaptic localization is a specialized neural context rather than the principal ERBB2 plasma-membrane localization. |
| GO:0045727 positive regulation of translation | IMP PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | KEEP AS NON CORE | Summary: Nuclear ERBB2 can promote cellular translation through RNA Pol I-driven rRNA transcription. Reason: The translation phenotype is downstream of the noncanonical nuclear ERBB2-Pol I function. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0045765 regulation of angiogenesis | NAS PMID:15609325 Identification and validation of novel ERBB2 (HER2, NEU) tar... | KEEP AS NON CORE | Summary: ERBB2 perturbation affects angiogenesis-associated targets in cancer cells. Reason: Angiogenesis regulation is an indirect cancer-signaling output and is kept as non-core. Supporting Evidence: PMID:15609325 Identification and validation of novel ERBB2 (HER2, NEU) targets including genes involved in angiogenesis. |
| GO:0045785 positive regulation of cell adhesion | IDA PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | KEEP AS NON CORE | Summary: ERBB2-ERBB3 signaling can promote cell adhesion phenotypes. Reason: Cell adhesion is a downstream cellular phenotype of ERBB receptor signaling. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0045943 positive regulation of transcription by RNA polymerase I | IMP PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activa... | KEEP AS NON CORE | Summary: Nuclear ERBB2 stimulates RNA polymerase I-dependent rRNA transcription. Reason: This is a supported but noncanonical nuclear transcriptional role rather than the primary receptor kinase activity. Supporting Evidence: PMID:21555369 Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes. |
| GO:0046330 positive regulation of JNK cascade | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB signaling can feed into the JNK cascade. Reason: JNK activation is a valid but secondary downstream route compared with ERBB2 kinase activity and MAPK/PI3K signaling. |
| GO:0046982 protein heterodimerization activity | IPI PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signali... | ACCEPT | Summary: ERBB2 heterodimerizes with ERBB3 to create active neuregulin receptor complexes. Reason: Protein heterodimerization with ERBB3 is an established molecular function of ERBB2. Supporting Evidence: PMID:7556068 Heregulin-dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3. |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: ERBB2 can localize to the perinuclear region during endosomal and retrograde trafficking. Reason: Perinuclear ERBB2 is a trafficking-associated localization and not the receptor's core signaling compartment. |
| GO:0050679 positive regulation of epithelial cell proliferation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: ERBB2 signaling promotes epithelial proliferation in ligand-responsive contexts. Reason: Epithelial proliferation is a downstream biological output of ERBB signaling rather than a direct receptor activity. |
| GO:0050679 positive regulation of epithelial cell proliferation | IDA PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | KEEP AS NON CORE | Summary: ERBB2 signaling promotes epithelial proliferation in ligand-responsive contexts. Reason: Epithelial proliferation is a downstream biological output of ERBB signaling rather than a direct receptor activity. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. Both ErbB-1 and ErbB-2 contribute significantly to tumorigenicity. |
| GO:0070372 regulation of ERK1 and ERK2 cascade | IMP PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry o... | KEEP AS NON CORE | Summary: ERBB2 nuclear transport intersects with ERK1/ERK2 signaling. Reason: ERK cascade regulation is a downstream output and this specific row was assayed in the nuclear-transport context. Supporting Evidence: PMID:16314522 Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. |
| GO:0071363 cellular response to growth factor stimulus | IDA PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migr... | KEEP AS NON CORE | Summary: ERBB2 responds to growth-factor stimulation through CPNE3-dependent trafficking and motility outputs. Reason: This is a growth-factor response phenotype linked to ERBB2 relocalization rather than the core kinase reaction. Supporting Evidence: PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migration. |
| GO:0071364 cellular response to epidermal growth factor stimulus | IMP PMID:27134172 Crystal Structure and Substrate Specificity of PTPN12. | KEEP AS NON CORE | Summary: EGF stimulation can activate ERBB2 through EGFR:ERBB2 heterodimers. Reason: The EGF-response term is correct for the EGFR:ERBB2 route but is stimulus-contextual. Supporting Evidence: PMID:27134172 Crystal Structure and Substrate Specificity of PTPN12. |
| GO:0071526 semaphorin-plexin signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB2 contributes to SEMA4D/Plexin-B1 signal transduction. Reason: Semaphorin-plexin signaling is a specialized ERBB2 coreceptor context, distinct from canonical ERBB ligand signaling. |
| GO:0071526 semaphorin-plexin signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: ERBB2 contributes to SEMA4D/Plexin-B1 signal transduction. Reason: Semaphorin-plexin signaling is a specialized ERBB2 coreceptor context, distinct from canonical ERBB ligand signaling. |
| GO:0090314 positive regulation of protein targeting to membrane | IDA PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migr... | KEEP AS NON CORE | Summary: CPNE3 links ERBB2 signaling to receptor targeting at the plasma membrane. Reason: Protein targeting to membrane is a downstream trafficking phenotype of CPNE3-ERBB2 signaling. Supporting Evidence: PMID:20010870 Copine-III interacts with ErbB2 and promotes tumor cell migration. |
| GO:0099645 neurotransmitter receptor localization to postsynaptic specialization membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ERBB orthology supports a neural receptor-localization output. Reason: This synaptic localization process is kept as a non-core inferred neural output of mammalian ERBB signaling. |
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