Epidermal growth factor receptor (EGFR/ERBB1/HER1) is a receptor tyrosine kinase (EC 2.7.10.1) that binds EGF family ligands (EGF, TGF-alpha, amphiregulin, betacellulin, epiregulin, epigen, HB-EGF) to initiate signal transduction cascades controlling cell proliferation, survival, differentiation, and migration. Upon ligand binding, EGFR undergoes homo- or heterodimerization (with ERBB2, ERBB3, ERBB4), which activates the intracellular tyrosine kinase domain through trans-autophosphorylation. Phosphorylated tyrosine residues in the C-terminal tail serve as docking sites for SH2/PTB domain-containing adaptor proteins (GRB2, SHC, etc.), leading to activation of RAS-RAF-MEK-ERK (MAPK), PI3K-AKT, PLCgamma-PKC, and STAT signaling pathways. EGFR localizes primarily to the plasma membrane and continues signaling from early endosomes after clathrin-mediated endocytosis. Receptor downregulation occurs through CBL-mediated ubiquitination and lysosomal degradation. EGFR mutations and overexpression drive multiple cancers including non-small cell lung cancer, colorectal cancer, and glioblastoma.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. Supporting Evidence: file:human/EGFR/EGFR-deep-research-falcon.md model: Edison Scientific Literature |
| GO:0043410 positive regulation of MAPK cascade | IBA GO_REF:0000033 | ACCEPT | Summary: EGFR positively regulates the MAPK cascade through recruitment of GRB2-SOS and activation of RAS-RAF-MEK-ERK signaling. Reason: MAPK/ERK pathway activation is a core downstream signaling output of EGFR. This is well-established. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: EGFR is a receptor tyrosine kinase (EC 2.7.10.1) that phosphorylates tyrosine residues on substrate proteins following ligand-induced dimerization. This is a core molecular function. Reason: Transmembrane receptor protein tyrosine kinase activity is the defining enzymatic function of EGFR. The kinase domain catalyzes ATP-dependent phosphorylation of tyrosine residues. |
| GO:0030182 neuron differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: EGFR signaling influences neuron differentiation, a downstream developmental effect. Reason: Neuron differentiation is a downstream developmental process influenced by EGFR signaling, not a core molecular function. |
| GO:0043066 negative regulation of apoptotic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: EGFR signaling promotes cell survival by activating anti-apoptotic pathways including PI3K-AKT. Reason: Anti-apoptotic effects are downstream consequences of EGFR-PI3K-AKT signaling, not a core function. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. |
| GO:0050679 positive regulation of epithelial cell proliferation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: EGFR signaling promotes epithelial cell proliferation, a key downstream effect in epithelial tissues. Reason: Epithelial cell proliferation is a major physiological outcome of EGFR signaling but represents a downstream effect. |
| GO:0043235 receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: EGFR forms homo- and heterodimeric receptor complexes upon ligand binding, which is required for kinase activation. Reason: EGFR dimerization into receptor complexes is essential for signal transduction. EGFR forms homodimers and heterodimers with ERBB2, ERBB3, ERBB4. |
| GO:0009925 basal plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: EGFR localizes to the basal plasma membrane in polarized cells. Reason: Basal plasma membrane localization is consistent with EGFR function in polarized cells. |
| GO:0048408 epidermal growth factor binding | IBA GO_REF:0000033 | ACCEPT | Summary: EGFR binds EGF through its extracellular domain (subdomains I and III), which induces receptor dimerization and activation. Reason: EGF binding is the canonical ligand-binding function of EGFR. Crystal structures confirm EGF binds domains I and III of the extracellular region. |
| GO:0000165 MAPK cascade | IEA GO_REF:0000108 | ACCEPT | Summary: EGFR participates in the MAPK cascade by activating RAS-RAF-MEK-ERK signaling upon ligand binding. Reason: MAPK cascade activation is a principal downstream effect of EGFR signaling. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR is a receptor tyrosine kinase (EC 2.7.10.1) that phosphorylates tyrosine residues on substrate proteins following ligand-induced dimerization. This is a core molecular function. Reason: Transmembrane receptor protein tyrosine kinase activity is the defining enzymatic function of EGFR. The kinase domain catalyzes ATP-dependent phosphorylation of tyrosine residues. |
| GO:0046718 symbiont entry into host cell | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: EGFR can serve as a receptor for viral entry, including some herpesviruses. Reason: Viral receptor function is not a normal physiological function of EGFR. |
| GO:0000139 Golgi membrane | IEA GO_REF:0000044 | ACCEPT | Summary: EGFR localizes to Golgi membranes during biosynthesis. Reason: Part of normal EGFR trafficking through the secretory pathway. |
| GO:0000166 nucleotide binding | IEA GO_REF:0000043 | ACCEPT | Summary: EGFR binds nucleotides (ATP) for its kinase activity. Reason: General parent term for ATP binding, accurate for EGFR. |
| GO:0001618 virus receptor activity | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: EGFR can act as a receptor for certain viruses. Reason: Virus receptor activity is not a core physiological function. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | ACCEPT | Summary: EGFR has protein kinase activity, phosphorylating protein substrates on tyrosine residues. Reason: Accurate parent term for the protein tyrosine kinase activity of EGFR. |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR binds ATP in its kinase domain active site to catalyze phosphorylation reactions. Reason: ATP binding is essential for EGFR kinase activity. The ATP-binding pocket in the kinase domain is the target of many therapeutic inhibitors. |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | ACCEPT | Summary: The EGFR extracellular domain is exposed to the extracellular region. Reason: The ligand-binding ectodomain of EGFR is in the extracellular region. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Nuclear EGFR has been described in certain contexts and may have transcriptional roles. Reason: Nuclear EGFR is documented but represents a minor, context-dependent localization rather than core EGFR function. |
| GO:0005768 endosome | IEA GO_REF:0000044 | ACCEPT | Summary: EGFR localizes to endosomes following ligand-induced internalization. EGFR continues signaling from early endosomes and is subsequently sorted for recycling or lysosomal degradation. Reason: Endosomal localization is part of normal EGFR trafficking and signaling. EGFR signals from endosomes and trafficking modulates signal duration. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: EGFR is synthesized and processed in the ER membrane. Reason: Part of normal EGFR biosynthesis in the secretory pathway. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: EGFR is a cell surface receptor protein tyrosine kinase that initiates signaling upon ligand binding. Reason: This is the parent pathway term that accurately describes EGFR function. |
| GO:0010008 endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: EGFR localizes to endosome membranes during receptor trafficking after internalization. Reason: After ligand-induced endocytosis, EGFR is found on endosome membranes where it continues to signal. |
| GO:0016020 membrane | IEA GO_REF:0000002 | ACCEPT | Summary: EGFR is a single-pass transmembrane protein with extracellular, transmembrane, and intracellular domains. The membrane localization is fundamental to its structure and function. Reason: As a transmembrane receptor, EGFR requires membrane localization for proper protein topology, with the extracellular domain for ligand binding and the intracellular kinase domain for signal transduction. |
| GO:0016301 kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR has kinase activity, a parent term of protein tyrosine kinase activity. Reason: This is a general parent term that accurately describes EGFR function, though more specific terms are preferred. |
| GO:0016740 transferase activity | IEA GO_REF:0000043 | ACCEPT | Summary: EGFR has transferase activity as it transfers phosphate groups from ATP to protein substrates. Reason: Very general parent term but accurate for EGFR kinase function. |
| GO:0031965 nuclear membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: EGFR has been reported at the nuclear membrane in certain contexts. Reason: Nuclear membrane localization is not a primary EGFR localization. |
| GO:0043235 receptor complex | IEA GO_REF:0000117 | ACCEPT | Summary: EGFR forms homo- and heterodimeric receptor complexes upon ligand binding, which is required for kinase activation. Reason: EGFR dimerization into receptor complexes is essential for signal transduction. EGFR forms homodimers and heterodimers with ERBB2, ERBB3, ERBB4. |
| GO:0070374 positive regulation of ERK1 and ERK2 cascade | IEA GO_REF:0000117 | ACCEPT | Summary: EGFR positively regulates ERK1/2 cascade through RAS-RAF-MEK-ERK signaling axis. Reason: ERK1/2 activation is a core readout of EGFR signaling through the MAPK pathway. |
| GO:0005515 protein binding | IPI PMID:10229072 Association of Nck with tyrosine-phosphorylated SLP-76 in ac... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:10229072 Association of Nck with tyrosine-phosphorylated SLP-76 in activated T lymphocytes. |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. |
| GO:0005515 protein binding | IPI PMID:10805725 Class II phosphoinositide 3-kinases are downstream targets o... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:10805725 Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors. |
| GO:0005515 protein binding | IPI PMID:11896612 Use of signal specific receptor tyrosine kinase oncoproteins... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:11896612 Use of signal specific receptor tyrosine kinase oncoproteins reveals that pathways downstream from Grb2 or Shc are sufficient for cell transformation and metastasis. |
| GO:0005515 protein binding | IPI PMID:12070153 Identification of both positive and negative domains within ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:12070153 2002 Jun 17. Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation. |
| GO:0005515 protein binding | IPI PMID:12297049 Crystal structure of a truncated epidermal growth factor rec... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:12297049 Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. |
| GO:0005515 protein binding | IPI PMID:12297050 Crystal structure of the complex of human epidermal growth f... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:12297050 Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:12577067 A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. |
| GO:0005515 protein binding | IPI PMID:12620237 EGF activates its receptor by removing interactions that aut... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:12620237 EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. |
| GO:0005515 protein binding | IPI PMID:14568990 Role of the pleckstrin homology domain of PLCgamma1 in its i... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:14568990 Oct 20. Role of the pleckstrin homology domain of PLCgamma1 in its interaction with the insulin receptor. |
| GO:0005515 protein binding | IPI PMID:14679214 A novel proteomic screen for peptide-protein interactions. | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:14679214 2003 Dec 16. A novel proteomic screen for peptide-protein interactions. |
| GO:0005515 protein binding | IPI PMID:14966128 Structural requirements for signal transducer and activator ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:14966128 2004 Feb 13. Structural requirements for signal transducer and activator of transcription 3 binding to phosphotyrosine ligands containing the YXXQ motif. |
| GO:0005515 protein binding | IPI PMID:15225635 Identification of 14-3-3zeta as an EGF receptor interacting ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:15225635 Identification of 14-3-3zeta as an EGF receptor interacting protein. |
| GO:0005515 protein binding | IPI PMID:15282549 LRIG1 restricts growth factor signaling by enhancing recepto... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:15282549 Jul 29. 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: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:15345710 2004 Sep 1. The leucine-rich repeat protein LRIG1 is a negative regulator of ErbB family receptor tyrosine kinases. |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:15657067 Epub 2005 Jan 17. Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. |
| GO:0005515 protein binding | IPI PMID:15962011 Sprouty2 acts at the Cbl/CIN85 interface to inhibit epiderma... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:15962011 Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation. |
| GO:0005515 protein binding | IPI PMID:16253990 Increased proliferation and altered growth factor dependence... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:16253990 Oct 27. Increased proliferation and altered growth factor dependence of human mammary epithelial cells overexpressing the Gab2 docking protein. |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays. |
| GO:0005515 protein binding | IPI PMID:16499958 Crystal structure of the ubiquitin binding domains of rabex-... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:16499958 Feb 23. Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. |
| GO:0005515 protein binding | IPI PMID:16516204 Activation of ErbB2 by 2-methyl-1,4-naphthoquinone (menadion... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:16516204 Epub 2006 Feb 28. 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:16799092 Dynamic profiling of the post-translational modifications an... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:16799092 Epub 2006 Jun 23. Dynamic profiling of the post-translational modifications and interaction partners of epidermal growth factor receptor signaling after stimulation by epidermal growth factor using Extended Range Proteomic Analysis (ERPA). |
| GO:0005515 protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:16914641 Intersectin regulates epidermal growth factor receptor endoc... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:16914641 Aug 16. Intersectin regulates epidermal growth factor receptor endocytosis, ubiquitylation, and signaling. |
| GO:0005515 protein binding | IPI PMID:16954185 Advanced glycation end product (AGE) receptor 1 suppresses c... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:16954185 Advanced glycation end product (AGE) receptor 1 suppresses cell oxidant stress and activation signaling via EGF receptor. |
| GO:0005515 protein binding | IPI PMID:17126326 Extracellular heat shock protein 70 mediates heat stress-ind... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17126326 Epub 2006 Nov 20. Extracellular heat shock protein 70 mediates heat stress-induced epidermal growth factor receptor transactivation in A431 carcinoma cells. |
| GO:0005515 protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:17284441 Epidermal growth factor directs sex-specific steroid signali... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17284441 2007 Feb 5. Epidermal growth factor directs sex-specific steroid signaling through Src activation. |
| GO:0005515 protein binding | IPI PMID:17403676 Rin1 interacts with signal-transducing adaptor molecule (STA... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17403676 2007 Apr 2. Rin1 interacts with signal-transducing adaptor molecule (STAM) and mediates epidermal growth factor receptor trafficking and degradation. |
| GO:0005515 protein binding | IPI PMID:17697999 Ligand-induced structural transitions in ErbB receptor extra... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17697999 Ligand-induced structural transitions in ErbB receptor extracellular domains. |
| GO:0005515 protein binding | IPI PMID:17726113 Inhibition of the leucine-rich repeat protein LINGO-1 enhanc... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17726113 Inhibition of the leucine-rich repeat protein LINGO-1 enhances survival, structure, and function of dopaminergic neurons in Parkinson's disease models. |
| GO:0005515 protein binding | IPI PMID:18046415 Inhibition of the EGF receptor by binding of MIG6 to an acti... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18046415 Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface. |
| GO:0005515 protein binding | IPI PMID:18273061 Structural basis for a novel intrapeptidyl H-bond and revers... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18273061 Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates. |
| GO:0005515 protein binding | IPI PMID:18455122 Survival of cancer cells is maintained by EGFR independent o... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18455122 Survival of cancer cells is maintained by EGFR independent of its kinase activity. |
| GO:0005515 protein binding | IPI PMID:18542056 LRIG1 negatively regulates the oncogenic EGF receptor mutant... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18542056 LRIG1 negatively regulates the oncogenic EGF receptor mutant EGFRvIII. |
| GO:0005515 protein binding | IPI PMID:18776048 Comparisons of tyrosine phosphorylated proteins in cells exp... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18776048 Comparisons of tyrosine phosphorylated proteins in cells expressing lung cancer-specific alleles of EGFR and KRAS. |
| GO:0005515 protein binding | IPI PMID:18824549 Acidic mammalian chitinase is secreted via an ADAM17/epiderm... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18824549 2008 Sep 29. Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth factor receptor-dependent pathway and stimulates chemokine production by pulmonary epithelial cells. |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:19167335 Large-scale structural analysis of the classical human protein tyrosine phosphatome. |
| GO:0005515 protein binding | IPI PMID:19172738 Phosphorylation-dependent binding of 14-3-3 terminates signa... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:19172738 Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein. |
| GO:0005515 protein binding | IPI PMID:19650109 Flow cytometric in situ proximity ligation analyses of prote... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:19798056 Participation of Tom1L1 in EGF-stimulated endocytosis of EGF... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:19798056 Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor. |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20029029 Regulation of epidermal growth factor receptor trafficking by lysine deacetylase HDAC6. |
| GO:0005515 protein binding | IPI PMID:20153921 EGFR and EGFRvIII interact with PUMA to inhibit mitochondria... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20153921 2010 Feb 13. EGFR and EGFRvIII interact with PUMA to inhibit mitochondrial translocalization of PUMA and PUMA-mediated apoptosis independent of EGFR kinase activity. |
| GO:0005515 protein binding | IPI PMID:20308550 The phosphatase and tensin homolog regulates epidermal growt... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20308550 The phosphatase and tensin homolog regulates epidermal growth factor receptor (EGFR) inhibitor response by targeting EGFR for degradation. |
| GO:0005515 protein binding | IPI PMID:20403327 TRP channel regulates EGFR signaling in hair morphogenesis a... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20403327 TRP channel regulates EGFR signaling in hair morphogenesis and skin barrier formation. |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome to inhibit glioblastoma cell transformation and migration. |
| GO:0005515 protein binding | IPI PMID:20562913 Differential roles of ERK and Akt pathways in regulation of ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20562913 Differential roles of ERK and Akt pathways in regulation of EGFR-mediated signaling and motility in prostate cancer cells. |
| GO:0005515 protein binding | IPI PMID:20624308 EGFR/Met association regulates EGFR TKI resistance in breast... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20624308 EGFR/Met association regulates EGFR TKI resistance in breast cancer. |
| GO:0005515 protein binding | IPI PMID:20935677 A positive feedback loop of ER-Ξ±36/EGFR promotes malignant g... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20935677 A positive feedback loop of ER-Ξ±36/EGFR promotes malignant growth of ER-negative breast cancer cells. |
| GO:0005515 protein binding | IPI PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedbac... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:21258405 Galectin-3 regulates MUC1 and EGFR cellular distribution and... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21258405 Galectin-3 regulates MUC1 and EGFR cellular distribution and EGFR downstream pathways in pancreatic cancer cells. |
| GO:0005515 protein binding | IPI PMID:21266349 EGFR nuclear translocation modulates DNA repair following ci... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21266349 2011 Jan 25. EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation treatment. |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:21278788 Translationally controlled tumor protein induces human breas... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21278788 Translationally controlled tumor protein induces human breast epithelial cell transformation through the activation of Src. |
| GO:0005515 protein binding | IPI PMID:21349850 MAPK scaffold IQGAP1 binds the EGF receptor and modulates it... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21349850 2011 Feb 24. MAPK scaffold IQGAP1 binds the EGF receptor and modulates its activation. |
| GO:0005515 protein binding | IPI PMID:21376233 Activation of multiple proto-oncogenic tyrosine kinases in b... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:21439278 Engineered epidermal growth factor mutants with faster bindi... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21439278 2011 Mar 23. Engineered epidermal growth factor mutants with faster binding on-rates correlate with enhanced receptor activation. |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21706016 Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. |
| GO:0005515 protein binding | IPI PMID:21822280 Simultaneous visualization of the extracellular and cytoplas... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21822280 Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor. |
| GO:0005515 protein binding | IPI PMID:21951318 Ligand-dependent differences in estrogen receptor beta-inter... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:21951318 Ligand-dependent differences in estrogen receptor beta-interacting proteins identified in lung adenocarcinoma cells corresponds to estrogenic responses. |
| GO:0005515 protein binding | IPI PMID:22411794 Hypoxia promotes ligand-independent EGF receptor signaling v... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:22411794 Hypoxia promotes ligand-independent EGF receptor signaling via hypoxia-inducible factor-mediated upregulation of caveolin-1. |
| GO:0005515 protein binding | IPI PMID:22439932 NKX2-1/TITF1/TTF-1-Induced ROR1 is required to sustain EGFR ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:22439932 NKX2-1/TITF1/TTF-1-Induced ROR1 is required to sustain EGFR survival signaling in lung adenocarcinoma. |
| GO:0005515 protein binding | IPI PMID:22939624 Quantitative analysis of HSP90-client interactions reveals p... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:22939624 Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition. |
| GO:0005515 protein binding | IPI PMID:23178489 The role of insulin-like growth factor binding protein-3 in ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23178489 The role of insulin-like growth factor binding protein-3 in the breast cancer cell response to DNA-damaging agents. |
| GO:0005515 protein binding | IPI PMID:23178716 SnoN/SkiL expression is modulated via arsenic trioxide-induc... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23178716 2012 Nov 21. SnoN/SkiL expression is modulated via arsenic trioxide-induced activation of the PI3K/AKT pathway in ovarian cancer cells. |
| GO:0005515 protein binding | IPI PMID:23273428 Insights into the aberrant activity of mutant EGFR kinase do... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23273428 Dec 27. Insights into the aberrant activity of mutant EGFR kinase domain and drug recognition. |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23397142 Epub 2013 Feb 8. Analysis of protein-protein interactions in cross-talk pathways reveals CRKL protein as a novel prognostic marker in hepatocellular carcinoma. |
| GO:0005515 protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23436906 Epub 2013 Feb 22. Parallel visualization of multiple protein complexes in individual cells in tumor tissue. |
| GO:0005515 protein binding | IPI PMID:23520446 Protein phosphorylation profiling using an in situ proximity... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23520446 Protein phosphorylation profiling using an in situ proximity ligation assay: phosphorylation of AURKA-elicited EGFR-Thr654 and EGFR-Ser1046 in lung cancer cells. |
| GO:0005515 protein binding | IPI PMID:23597562 Inhibition of tumor angiogenesis and growth by a small-molec... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23597562 Inhibition of tumor angiogenesis and growth by a small-molecule multi-FGF receptor blocker with allosteric properties. |
| GO:0005515 protein binding | IPI PMID:23636329 EGFR modulates microRNA maturation in response to hypoxia th... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23636329 EGFR modulates microRNA maturation in response to hypoxia through phosphorylation of AGO2. |
| GO:0005515 protein binding | IPI PMID:23764002 Epidermal growth factor receptor potentiates MCM7-mediated D... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23764002 Epidermal growth factor receptor potentiates MCM7-mediated DNA replication through tyrosine phosphorylation of Lyn kinase in human cancers. |
| GO:0005515 protein binding | IPI PMID:23799367 Threshold-controlled ubiquitination of the EGFR directs rece... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23799367 Threshold-controlled ubiquitination of the EGFR directs receptor fate. |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:24034250 EGFR-mediated Beclin 1 phosphorylation in autophagy suppress... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:24034250 EGFR-mediated Beclin 1 phosphorylation in autophagy suppression, tumor progression, and tumor chemoresistance. |
| GO:0005515 protein binding | IPI PMID:24076656 Endophilin, Lamellipodin, and Mena cooperate to regulate F-a... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:24076656 Endophilin, Lamellipodin, and Mena cooperate to regulate F-actin-dependent EGF-receptor endocytosis. |
| GO:0005515 protein binding | IPI PMID:24135280 EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 a... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:24135280 EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 and progression in glioblastoma. |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:24189400 Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms. |
| GO:0005515 protein binding | IPI PMID:24557338 Characterisation of HER heterodimers in breast cancer using ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:24780295 Importance of EGFR/ERCC1 interaction following radiation-ind... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:24780295 Importance of EGFR/ERCC1 interaction following radiation-induced DNA damage. |
| GO:0005515 protein binding | IPI PMID:24947832 Differential protein-protein interactions of LRRK1 and LRRK2... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:24947832 Differential protein-protein interactions of LRRK1 and LRRK2 indicate roles in distinct cellular signaling pathways. |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25036637 A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. |
| GO:0005515 protein binding | IPI PMID:25136068 Mycoplasma hyorhinis infection promotes NF-ΞΊB-dependent migr... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25136068 Epub 2014 Aug 18. Mycoplasma hyorhinis infection promotes NF-ΞΊB-dependent migration of gastric cancer cells. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25241761 Oct 9. Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network. |
| GO:0005515 protein binding | IPI PMID:25353163 Soluble LRIG2 ectodomain is released from glioblastoma cells... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25353163 eCollection 2014. Soluble LRIG2 ectodomain is released from glioblastoma cells and promotes the proliferation and inhibits the apoptosis of glioblastoma cells in vitro and in vivo in a similar manner to the full-length LRIG2. |
| GO:0005515 protein binding | IPI PMID:25594178 A kinase-independent role for EGF receptor in autophagy init... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25594178 A kinase-independent role for EGF receptor in autophagy initiation. |
| GO:0005515 protein binding | IPI PMID:25796184 PEA-15 facilitates EGFR dephosphorylation via ERK sequestrat... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25796184 2015 Mar 18. PEA-15 facilitates EGFR dephosphorylation via ERK sequestration at increased ER-PM contacts in TNBC cells. |
| GO:0005515 protein binding | IPI PMID:25873175 AXL mediates resistance to PI3KΞ± inhibition by activating th... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25873175 AXL mediates resistance to PI3KΞ± inhibition by activating the EGFR/PKC/mTOR axis in head and neck and esophageal squamous cell carcinomas. |
| GO:0005515 protein binding | IPI PMID:25970784 PTPRG suppresses tumor growth and invasion via inhibition of... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25970784 PTPRG suppresses tumor growth and invasion via inhibition of Akt signaling in nasopharyngeal carcinoma. |
| GO:0005515 protein binding | IPI PMID:26005835 RasGRP1 opposes proliferative EGFR-SOS1-Ras signals and rest... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:26005835 RasGRP1 opposes proliferative EGFR-SOS1-Ras signals and restricts intestinal epithelial cell growth. |
| GO:0005515 protein binding | IPI PMID:26280537 Secreted and O-GlcNAcylated MIF binds to the human EGF recep... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:26280537 Secreted and O-GlcNAcylated MIF binds to the human EGF receptor and inhibits its activation. |
| GO:0005515 protein binding | IPI PMID:26551075 EGF-receptor specificity for phosphotyrosine-primed substrat... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:26551075 Nov 9. EGF-receptor specificity for phosphotyrosine-primed substrates provides signal integration with Src. |
| GO:0005515 protein binding | IPI PMID:26751287 The LINK-A lncRNA activates normoxic HIF1Ξ± signalling in tri... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:26751287 The LINK-A lncRNA activates normoxic HIF1Ξ± signalling in triple-negative breast cancer. |
| GO:0005515 protein binding | IPI PMID:27059931 Weak binding to E3 ubiquitin ligase c-Cbl increases EGFRvA p... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:27059931 Apr 16. Weak binding to E3 ubiquitin ligase c-Cbl increases EGFRvA protein stability. |
| GO:0005515 protein binding | IPI PMID:27569582 GOLM1 Modulates EGFR/RTK Cell-Surface Recycling to Drive Hep... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:27569582 2016 Aug 25. GOLM1 Modulates EGFR/RTK Cell-Surface Recycling to Drive Hepatocellular Carcinoma Metastasis. |
| GO:0005515 protein binding | IPI PMID:2790960 Functional independence of the epidermal growth factor recep... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:2790960 Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:27956147 2016 Dec 9. Systematic Identification of Oncogenic EGFR Interaction Partners. |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:28065597 2017 Jan 5. A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome. |
| GO:0005515 protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:28988771 2017 Oct 5. EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics. |
| GO:0005515 protein binding | IPI PMID:29455656 The E3 ubiquitin ligase NEDD4 mediates cell migration signal... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:29455656 The E3 ubiquitin ligase NEDD4 mediates cell migration signaling of EGFR in lung cancer cells. |
| GO:0005515 protein binding | IPI PMID:29844572 RANK-c attenuates aggressive properties of ER-negative breas... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:29844572 May 29. RANK-c attenuates aggressive properties of ER-negative breast cancer by inhibiting NF-ΞΊB activation and EGFR signaling. |
| GO:0005515 protein binding | IPI PMID:30083275 The S100A4 Protein Signals through the ErbB4 Receptor to Pro... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:30083275 The S100A4 Protein Signals through the ErbB4 Receptor to Promote Neuronal Survival. |
| GO:0005515 protein binding | IPI PMID:30662352 COPI-Mediated Nuclear Translocation of EGFRvIII Promotes STA... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:30662352 COPI-Mediated Nuclear Translocation of EGFRvIII Promotes STAT3 Phosphorylation and PKM2 Nuclear Localization. |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites. |
| GO:0005515 protein binding | IPI PMID:31862538 Neuropeptide bombesin receptor activation stimulates growth ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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:33420426 AXL is a candidate receptor for SARS-CoV-2 that promotes inf... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:33420426 Jan 8. AXL is a candidate receptor for SARS-CoV-2 that promotes infection of pulmonary and bronchial epithelial cells. |
| GO:0005515 protein binding | IPI PMID:34591612 A protein interaction landscape of breast cancer. | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:34591612 Oct 1. A protein interaction landscape of breast cancer. |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:34591642 Oct 1. A protein network map of head and neck cancer reveals PIK3CA mutant drug sensitivity. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. 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: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:35512704 2022 May 4. Systematic discovery of mutation-directed neo-protein-protein interactions in cancer. |
| GO:0005515 protein binding | IPI PMID:37100772 Large-scale phage-based screening reveals extensive pan-vira... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:37100772 Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs. |
| GO:0005515 protein binding | IPI PMID:7518560 Hierarchy of binding sites for Grb2 and Shc on the epidermal... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:7518560 Hierarchy of binding sites for Grb2 and Shc on the epidermal growth factor receptor. |
| GO:0005515 protein binding | IPI PMID:7542744 The phosphotyrosine interaction domain of Shc binds an LXNPX... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:7542744 The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor. |
| GO:0005515 protein binding | IPI PMID:7657591 Tyrosine phosphorylation of the c-cbl proto-oncogene protein... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:7657591 Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation. |
| GO:0005515 protein binding | IPI PMID:7685104 Substrate specificity of the protein tyrosine phosphatases. | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:7685104 Substrate specificity of the protein tyrosine phosphatases. |
| GO:0005515 protein binding | IPI PMID:7693694 Sequence specificity in recognition of the epidermal growth ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:7693694 Sequence specificity in recognition of the epidermal growth factor receptor by protein tyrosine phosphatase 1B. |
| GO:0005515 protein binding | IPI PMID:7797556 Src phosphorylation of the epidermal growth factor receptor ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:7797556 Src phosphorylation of the epidermal growth factor receptor at novel sites mediates receptor interaction with Src and P85 alpha. |
| GO:0005515 protein binding | IPI PMID:7993895 Identification of amino acids in the N-terminal SH2 domain o... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:7993895 Identification of amino acids in the N-terminal SH2 domain of phospholipase C gamma 1 important in the interaction with epidermal growth factor receptor. |
| GO:0005515 protein binding | IPI PMID:8034616 Tyrosines 1148 and 1173 of activated human epidermal growth ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:8034616 Tyrosines 1148 and 1173 of activated human epidermal growth factor receptors are binding sites of Shc in intact cells. |
| GO:0005515 protein binding | IPI PMID:8621392 Determinants of substrate recognition in the protein-tyrosin... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:8621392 Determinants of substrate recognition in the protein-tyrosine phosphatase, PTP1. |
| GO:0005515 protein binding | IPI PMID:8887653 The phosphotyrosine interaction domains of X11 and FE65 bind... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:8887653 The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. |
| GO:0005515 protein binding | IPI PMID:8940013 The Grb2-mSos1 complex binds phosphopeptides with higher aff... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:8940013 The Grb2-mSos1 complex binds phosphopeptides with higher affinity than Grb2. |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9020117 Subsets of epidermal growth factor receptors during activation and endocytosis. |
| GO:0005515 protein binding | IPI PMID:9050838 Development of "substrate-trapping" mutants to identify phys... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9050838 Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases. |
| GO:0005515 protein binding | IPI PMID:9135143 Activation of HER4 by heparin-binding EGF-like growth factor... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9135143 Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation. |
| GO:0005515 protein binding | IPI PMID:9355745 Protein tyrosine phosphatase 1B interacts with and is tyrosi... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9355745 Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor. |
| GO:0005515 protein binding | IPI PMID:9506989 Grb10 interacts differentially with the insulin receptor, in... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9506989 Grb10 interacts differentially with the insulin receptor, insulin-like growth factor I receptor, and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the pleckstrin homology and SH2 domains. |
| GO:0005515 protein binding | IPI PMID:9544989 Shc phosphotyrosine-binding domain dominantly interacts with... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9544989 Shc phosphotyrosine-binding domain dominantly interacts with epidermal growth factor receptors and mediates Ras activation in intact cells. |
| GO:0042802 identical protein binding | IPI PMID:16777603 An allosteric mechanism for activation of the kinase domain ... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:16777603 An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. |
| GO:0042802 identical protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. 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:18042729 Epidermal growth factor receptor juxtamembrane region regula... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:18042729 Epidermal growth factor receptor juxtamembrane region regulates allosteric tyrosine kinase activation. |
| GO:0042802 identical protein binding | IPI PMID:19563760 Mechanism for activation of the EGF receptor catalytic domai... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:19563760 Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment. |
| GO:0042802 identical protein binding | IPI PMID:19650109 Flow cytometric in situ proximity ligation analyses of prote... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. 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:20007378 Structural analysis of the catalytically inactive kinase dom... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:20007378 Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. |
| GO:0042802 identical protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:20029029 Regulation of epidermal growth factor receptor trafficking by lysine deacetylase HDAC6. |
| GO:0042802 identical protein binding | IPI PMID:20359299 A proximity ligation assay using transiently transfected, ep... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:20359299 A proximity ligation assay using transiently transfected, epitope-tagged proteins: application for in situ detection of dimerized receptor tyrosine kinases. |
| GO:0042802 identical protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquired ERK dependency in HER2-overexpressing breast cancer. |
| GO:0042802 identical protein binding | IPI PMID:21480528 Comparative analysis of fluorescence resonance energy transf... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:21480528 Apr 8. Comparative analysis of fluorescence resonance energy transfer (FRET) and proximity ligation assay (PLA). |
| GO:0042802 identical protein binding | IPI PMID:21482778 Quantification of receptor tyrosine kinase transactivation t... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:21482778 Quantification of receptor tyrosine kinase transactivation through direct dimerization and surface density measurements in single cells. |
| GO:0042802 identical protein binding | IPI PMID:22232519 In situ analysis of mutant EGFRs prevalent in glioblastoma m... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:22232519 Epub 2012 Jan 9. In situ analysis of mutant EGFRs prevalent in glioblastoma multiforme reveals aberrant dimerization, activation, and differential response to anti-EGFR targeted therapy. |
| GO:0042802 identical protein binding | IPI PMID:22579287 Oncogenic mutations counteract intrinsic disorder in the EGF... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:22579287 Oncogenic mutations counteract intrinsic disorder in the EGFR kinase and promote receptor dimerization. |
| GO:0042802 identical protein binding | IPI PMID:23273428 Insights into the aberrant activity of mutant EGFR kinase do... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:23273428 Dec 27. Insights into the aberrant activity of mutant EGFR kinase domain and drug recognition. |
| GO:0042802 identical protein binding | IPI PMID:23374349 Conformational coupling across the plasma membrane in activa... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:23374349 Conformational coupling across the plasma membrane in activation of the EGF receptor. |
| GO:0042802 identical protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:23436906 Epub 2013 Feb 22. Parallel visualization of multiple protein complexes in individual cells in tumor tissue. |
| GO:0042802 identical protein binding | IPI PMID:23636329 EGFR modulates microRNA maturation in response to hypoxia th... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:23636329 EGFR modulates microRNA maturation in response to hypoxia through phosphorylation of AGO2. |
| GO:0042802 identical protein binding | IPI PMID:24135280 EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 a... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:24135280 EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 and progression in glioblastoma. |
| GO:0042802 identical protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:28988771 2017 Oct 5. EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics. |
| GO:0042802 identical protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D). |
| GO:0042802 identical protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:35512704 2022 May 4. Systematic discovery of mutation-directed neo-protein-protein interactions in cancer. |
| GO:0042802 identical protein binding | IPI PMID:38572507 DRD1 suppresses cell proliferation and reduces EGFR activati... | ACCEPT | Summary: EGFR undergoes homodimerization, binding to itself as part of the activation mechanism. Reason: EGFR homodimerization is essential for kinase activation. Ligand binding promotes EGFR-EGFR homodimer formation. Supporting Evidence: PMID:38572507 Apr 4. DRD1 suppresses cell proliferation and reduces EGFR activation and PD-L1 expression in NSCLC. |
| GO:0007165 signal transduction | TAS Reactome:R-HSA-212718 | ACCEPT | Summary: EGFR mediates signal transduction from extracellular growth factors to intracellular signaling cascades. Reason: Signal transduction is a core function of EGFR as a receptor tyrosine kinase. |
| GO:0007173 epidermal growth factor receptor signaling pathway | TAS Reactome:R-HSA-177929 | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. |
| GO:0042059 negative regulation of epidermal growth factor receptor signaling pathway | TAS Reactome:R-HSA-182971 | ACCEPT | Summary: EGFR participates in negative regulation of its own signaling through internalization and degradation mechanisms. Reason: EGFR signaling is subject to negative feedback through receptor internalization, ubiquitination by CBL, and lysosomal degradation. |
| GO:0000902 cell morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling influences cell morphogenesis. Reason: Cell morphogenesis is a downstream developmental effect. |
| GO:0001892 embryonic placenta development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling contributes to embryonic placenta development. Reason: Developmental process downstream of EGFR signaling in specific tissues. |
| GO:0001942 hair follicle development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling is required for hair follicle development. Reason: Tissue-specific developmental process regulated by EGFR. |
| GO:0005006 epidermal growth factor receptor activity | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. |
| GO:0006511 ubiquitin-dependent protein catabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR undergoes ubiquitin-dependent degradation. Reason: EGFR is ubiquitinated and degraded, but this describes its regulation rather than function. |
| GO:0007165 signal transduction | IEA GO_REF:0000107 | ACCEPT | Summary: EGFR mediates signal transduction from extracellular growth factors to intracellular signaling cascades. Reason: Signal transduction is a core function of EGFR as a receptor tyrosine kinase. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. |
| GO:0007435 salivary gland morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling contributes to salivary gland development. Reason: Tissue-specific developmental process. |
| GO:0008283 cell population proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling influences cell proliferation. Reason: Cell proliferation is a downstream effect of EGFR activation. |
| GO:0008284 positive regulation of cell population proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling promotes cell proliferation through MAPK and PI3K pathways. Reason: Cell proliferation is a downstream phenotypic effect of EGFR signaling. |
| GO:0008544 epidermis development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling is critical for epidermis development. Reason: Developmental process in EGFR's namesake tissue, but represents downstream effects. |
| GO:0009986 cell surface | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR localizes to the cell surface where it is accessible for ligand binding. Reason: Cell surface localization is consistent with EGFR function as a receptor for extracellular growth factors. |
| GO:0010467 gene expression | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling regulates gene expression. Reason: Gene expression regulation is a downstream effect of EGFR signaling. |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: In polarized epithelial cells, EGFR localizes to the basolateral plasma membrane. Reason: EGFR shows polarized distribution in epithelial cells, localizing to basolateral membranes. |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR is ubiquitinated by CBL for endocytosis and degradation. Reason: Describes EGFR regulation, not its enzymatic function. |
| GO:0021795 cerebral cortex cell migration | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling influences cortical cell migration during development. Reason: Developmental process in the nervous system. |
| GO:0030139 endocytic vesicle | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR is internalized via endocytic vesicles following ligand binding. Reason: Endocytic vesicle localization is part of normal EGFR internalization. |
| GO:0038134 ERBB2-EGFR signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR heterodimerizes with ERBB2 to form signaling complexes with distinct downstream effects. Reason: EGFR-ERBB2 heterodimers are an important signaling unit with enhanced signaling capacity. |
| GO:0042059 negative regulation of epidermal growth factor receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR participates in negative regulation of its own signaling through internalization and degradation mechanisms. Reason: EGFR signaling is subject to negative feedback through receptor internalization, ubiquitination by CBL, and lysosomal degradation. |
| GO:0042127 regulation of cell population proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR regulates cell proliferation through downstream signaling. Reason: General cell proliferation regulation is a downstream effect. |
| GO:0042908 xenobiotic transport | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: EGFR involvement in xenobiotic transport is not well-established. Reason: This annotation is likely over-interpretation; EGFR is not a transporter. |
| GO:0045742 positive regulation of epidermal growth factor receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: EGFR itself positively regulates the EGF receptor signaling pathway as the initiating receptor. Reason: EGFR activation initiates and sustains EGF receptor signaling. |
| GO:0048146 positive regulation of fibroblast proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling promotes fibroblast proliferation. Reason: Cell type-specific downstream effect. |
| GO:0048408 epidermal growth factor binding | IEA GO_REF:0000107 | ACCEPT | Summary: EGFR binds EGF through its extracellular domain (subdomains I and III), which induces receptor dimerization and activation. Reason: EGF binding is the canonical ligand-binding function of EGFR. Crystal structures confirm EGF binds domains I and III of the extracellular region. |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: EGFR may localize to perinuclear regions during trafficking. Reason: Perinuclear localization may occur during endocytic trafficking. |
| GO:0048546 digestive tract morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling influences digestive tract development. Reason: Developmental process downstream of EGFR signaling. |
| GO:0050673 epithelial cell proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR promotes epithelial cell proliferation. Reason: Cell type-specific proliferation effect. |
| GO:0050679 positive regulation of epithelial cell proliferation | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: EGFR signaling promotes epithelial cell proliferation, a key downstream effect in epithelial tissues. Reason: Epithelial cell proliferation is a major physiological outcome of EGFR signaling but represents a downstream effect. |
| GO:0060571 morphogenesis of an epithelial fold | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling contributes to epithelial fold morphogenesis. Reason: Developmental morphogenesis process. |
| GO:0061029 eyelid development in camera-type eye | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling is involved in eyelid development. Reason: Tissue-specific developmental process. |
| GO:0070086 ubiquitin-dependent endocytosis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR undergoes ubiquitin-dependent endocytosis. Reason: Describes EGFR trafficking/regulation. |
| GO:0071230 cellular response to amino acid stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling responds to amino acid availability. Reason: Amino acid response is a contextual regulatory effect. |
| GO:0071363 cellular response to growth factor stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR mediates cellular responses to growth factors. Reason: General growth factor response is downstream of receptor activation. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | TAS Reactome:R-HSA-177930 | ACCEPT | Summary: EGFR is a receptor tyrosine kinase (EC 2.7.10.1) that phosphorylates tyrosine residues on substrate proteins following ligand-induced dimerization. This is a core molecular function. Reason: Transmembrane receptor protein tyrosine kinase activity is the defining enzymatic function of EGFR. The kinase domain catalyzes ATP-dependent phosphorylation of tyrosine residues. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | TAS Reactome:R-HSA-177933 | ACCEPT | Summary: EGFR is a receptor tyrosine kinase (EC 2.7.10.1) that phosphorylates tyrosine residues on substrate proteins following ligand-induced dimerization. This is a core molecular function. Reason: Transmembrane receptor protein tyrosine kinase activity is the defining enzymatic function of EGFR. The kinase domain catalyzes ATP-dependent phosphorylation of tyrosine residues. |
| GO:0005515 protein binding | IPI PMID:39073202 SNX32 Regulates Sorting and Trafficking of Activated EGFR to... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:39073202 SNX32 Regulates Sorting and Trafficking of Activated EGFR to the Lysosomal Degradation Pathway. |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:12828935 Activation of epidermal growth factor receptor signals induc... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:12828935 Activation of epidermal growth factor receptor signals induction of nitric oxide synthase-2 in human optic nerve head astrocytes in glaucomatous optic neuropathy. |
| GO:0005886 plasma membrane | IDA PMID:20462955 A G{alpha}i-GIV molecular complex binds epidermal growth fac... | ACCEPT | Summary: EGFR is a transmembrane receptor tyrosine kinase that localizes to the plasma membrane where it binds EGF ligands and undergoes dimerization and autophosphorylation to initiate downstream signaling cascades. Reason: Plasma membrane localization is essential for EGFR function as a transmembrane receptor that needs to be at the cell surface to bind extracellular EGF ligands and interact with other membrane-bound signaling components. Supporting Evidence: PMID:20462955 2010 May 12. A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor and determines whether cells migrate or proliferate. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0005768 endosome | IDA PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | ACCEPT | Summary: EGFR localizes to endosomes following ligand-induced internalization. EGFR continues signaling from early endosomes and is subsequently sorted for recycling or lysosomal degradation. Reason: Endosomal localization is part of normal EGFR trafficking and signaling. EGFR signals from endosomes and trafficking modulates signal duration. Supporting Evidence: PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediated inactivation of the EGF receptor. |
| GO:0019900 kinase binding | IPI PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | ACCEPT | Summary: EGFR binds to kinases including SRC family kinases and downstream signaling kinases. Reason: EGFR interacts with multiple kinases in signaling complexes. Supporting Evidence: PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediated inactivation of the EGF receptor. |
| GO:0090037 positive regulation of protein kinase C signaling | IDA PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | KEEP AS NON CORE | Summary: EGFR activates PKC signaling through PLC-gamma activation. Reason: PKC signaling regulation is downstream of EGFR-PLC-gamma activation. Supporting Evidence: PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediated inactivation of the EGF receptor. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IMP PMID:18483258 UVA-induced cell cycle progression is mediated by a disinteg... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:18483258 UVA-induced cell cycle progression is mediated by a disintegrin and metalloprotease/epidermal growth factor receptor/AKT/Cyclin D1 pathways in keratinocytes. |
| GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction | IMP PMID:18483258 UVA-induced cell cycle progression is mediated by a disinteg... | KEEP AS NON CORE | Summary: EGFR activates PI3K-AKT signaling through recruitment of PI3K to phosphotyrosine docking sites. Reason: PI3K-AKT pathway activation is a major downstream signaling axis of EGFR, but is not the core function. Supporting Evidence: PMID:18483258 UVA-induced cell cycle progression is mediated by a disintegrin and metalloprotease/epidermal growth factor receptor/AKT/Cyclin D1 pathways in keratinocytes. |
| GO:1900087 positive regulation of G1/S transition of mitotic cell cycle | IMP PMID:18483258 UVA-induced cell cycle progression is mediated by a disinteg... | KEEP AS NON CORE | Summary: EGFR signaling promotes G1/S cell cycle transition. Reason: Cell cycle regulation is a downstream effect of EGFR proliferative signaling. Supporting Evidence: PMID:18483258 UVA-induced cell cycle progression is mediated by a disintegrin and metalloprotease/epidermal growth factor receptor/AKT/Cyclin D1 pathways in keratinocytes. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:24854121 2014 May 20. Endophilin-1 regulates blood-brain barrier permeability by controlling ZO-1 and occludin expression via the EGFR-ERK1/2 pathway. |
| GO:0043410 positive regulation of MAPK cascade | IDA PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | ACCEPT | Summary: EGFR positively regulates the MAPK cascade through recruitment of GRB2-SOS and activation of RAS-RAF-MEK-ERK signaling. Reason: MAPK/ERK pathway activation is a core downstream signaling output of EGFR. This is well-established. Supporting Evidence: PMID:24854121 2014 May 20. Endophilin-1 regulates blood-brain barrier permeability by controlling ZO-1 and occludin expression via the EGFR-ERK1/2 pathway. |
| GO:0005794 Golgi apparatus | IDA GO_REF:0000052 | ACCEPT | Summary: EGFR transits through the Golgi during biosynthesis and trafficking. Reason: EGFR is processed through the secretory pathway including the Golgi. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: EGFR cytoplasmic domain resides in the cytosol and signals to cytosolic proteins. Reason: The intracellular kinase domain of EGFR is in the cytosol. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005929 cilium | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: EGFR has been detected in cilia. Reason: Ciliary localization is context-specific. |
| GO:0030054 cell junction | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: EGFR may localize to cell junctions. Reason: Cell junction localization is context-dependent. |
| GO:0036064 ciliary basal body | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: EGFR has been detected at ciliary basal bodies. Reason: Ciliary localization is context-specific. |
| GO:0097225 sperm midpiece | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: EGFR has been detected in sperm midpiece. Reason: Sperm-specific localization. |
| GO:0097228 sperm principal piece | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: EGFR has been detected in sperm principal piece. Reason: Sperm-specific localization. |
| GO:0097229 sperm end piece | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: EGFR has been detected in sperm end piece. Reason: Sperm-specific localization. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-177934 | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-182969 | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-183058 | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-212710 | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-8867041 | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. |
| GO:0005515 protein binding | IPI PMID:15611079 Epigen, the last ligand of ErbB receptors, reveals intricate... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:15611079 Dec 17. Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:12828935 Activation of epidermal growth factor receptor signals induc... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:12828935 Activation of epidermal growth factor receptor signals induction of nitric oxide synthase-2 in human optic nerve head astrocytes in glaucomatous optic neuropathy. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IMP PMID:17655843 EGF receptor transactivation and PI3-kinase mediate stimulat... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:17655843 EGF receptor transactivation and PI3-kinase mediate stimulation of ERK by alpha(2A)-adrenoreceptor in intestinal epithelial cells: a role in wound healing. |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | IMP PMID:17655843 EGF receptor transactivation and PI3-kinase mediate stimulat... | KEEP AS NON CORE | Summary: EGFR positively regulates PI3K-AKT signaling. Reason: PI3K-AKT regulation is downstream of EGFR activation. Supporting Evidence: PMID:17655843 EGF receptor transactivation and PI3-kinase mediate stimulation of ERK by alpha(2A)-adrenoreceptor in intestinal epithelial cells: a role in wound healing. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177935 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8863804 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864029 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:1902895 positive regulation of miRNA transcription | IMP PMID:21673316 TRPS1 targeting by miR-221/222 promotes the epithelial-to-me... | KEEP AS NON CORE | Summary: EGFR signaling regulates miRNA transcription. Reason: miRNA regulation is a downstream transcriptional effect. Supporting Evidence: PMID:21673316 TRPS1 targeting by miR-221/222 promotes the epithelial-to-mesenchymal transition in breast cancer. |
| GO:0005886 plasma membrane | IDA PMID:15611079 Epigen, the last ligand of ErbB receptors, reveals intricate... | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. Supporting Evidence: PMID:15611079 Dec 17. Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:2472218 EGF induces tyrosine phosphorylation of phospholipase C-II: ... | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. Supporting Evidence: PMID:2472218 EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling. |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) receptor and ErbB2 and the affinity of EGF binding are regulated by different mechanisms. |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF recep... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma. |
| GO:0005886 plasma membrane | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. Supporting Evidence: PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) receptor and ErbB2 and the affinity of EGF binding are regulated by different mechanisms. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:9890893 Identification of tyrosine phosphorylation sites in human Ga... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:9890893 Identification of tyrosine phosphorylation sites in human Gab-1 protein by EGF receptor kinase in vitro. |
| GO:0038134 ERBB2-EGFR signaling pathway | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR heterodimerizes with ERBB2 to form signaling complexes with distinct downstream effects. Reason: EGFR-ERBB2 heterodimers are an important signaling unit with enhanced signaling capacity. Supporting Evidence: PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) receptor and ErbB2 and the affinity of EGF binding are regulated by different mechanisms. |
| GO:0005515 protein binding | IPI PMID:27872189 Biophysical Evidence for Intrinsic Disorder in the C-termina... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:27872189 2016 Nov 21. Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:9890893 Identification of tyrosine phosphorylation sites in human Ga... | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. Supporting Evidence: PMID:9890893 Identification of tyrosine phosphorylation sites in human Gab-1 protein by EGF receptor kinase in vitro. |
| GO:0030296 protein tyrosine kinase activator activity | IDA PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF recep... | ACCEPT | Summary: EGFR can activate other tyrosine kinases through heterodimerization (especially ERBB2). Reason: EGFR activates ERBB2 kinase activity through heterodimer formation. Supporting Evidence: PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma. |
| GO:0030296 protein tyrosine kinase activator activity | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR can activate other tyrosine kinases through heterodimerization (especially ERBB2). Reason: EGFR activates ERBB2 kinase activity through heterodimer formation. Supporting Evidence: PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) receptor and ErbB2 and the affinity of EGF binding are regulated by different mechanisms. |
| GO:0005886 plasma membrane | IDA PMID:11331309 Real time fluorescence imaging of PLC gamma translocation an... | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. Supporting Evidence: PMID:11331309 Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor. |
| GO:0032587 ruffle membrane | IDA PMID:11331309 Real time fluorescence imaging of PLC gamma translocation an... | KEEP AS NON CORE | Summary: EGFR localizes to membrane ruffles during cell migration. Reason: Ruffle localization is associated with EGFR-induced cell migration. Supporting Evidence: PMID:11331309 Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor. |
| GO:0097708 intracellular vesicle | IDA PMID:11331309 Real time fluorescence imaging of PLC gamma translocation an... | ACCEPT | Summary: EGFR is found in intracellular vesicles during trafficking. Reason: Part of EGFR endocytic trafficking. Supporting Evidence: PMID:11331309 Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor. |
| GO:0005515 protein binding | IPI PMID:17334392 A crucial role of plasma membrane-associated sialidase in th... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17334392 Mar 5. A crucial role of plasma membrane-associated sialidase in the survival of human cancer cells. |
| GO:0019900 kinase binding | IPI PMID:18722344 BCAR3 regulates EGF-induced DNA synthesis in normal human br... | ACCEPT | Summary: EGFR binds to kinases including SRC family kinases and downstream signaling kinases. Reason: EGFR interacts with multiple kinases in signaling complexes. Supporting Evidence: PMID:18722344 BCAR3 regulates EGF-induced DNA synthesis in normal human breast MCF-12A cells. |
| GO:0005515 protein binding | IPI PMID:26988023 Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facil... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:26988023 Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance. |
| GO:0005515 protein binding | IPI PMID:25187647 Structural basis for activation of trimeric Gi proteins by m... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25187647 2014 Sep 3. Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin. |
| GO:0005515 protein binding | IPI PMID:18722344 BCAR3 regulates EGF-induced DNA synthesis in normal human br... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18722344 BCAR3 regulates EGF-induced DNA synthesis in normal human breast MCF-12A cells. |
| GO:0005515 protein binding | IPI PMID:20462955 A G{alpha}i-GIV molecular complex binds epidermal growth fac... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20462955 2010 May 12. A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor and determines whether cells migrate or proliferate. |
| GO:0005515 protein binding | IPI PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:24854121 2014 May 20. Endophilin-1 regulates blood-brain barrier permeability by controlling ZO-1 and occludin expression via the EGFR-ERK1/2 pathway. |
| GO:0048471 perinuclear region of cytoplasm | IMP PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | KEEP AS NON CORE | Summary: EGFR may localize to perinuclear regions during trafficking. Reason: Perinuclear localization may occur during endocytic trafficking. Supporting Evidence: PMID:24854121 2014 May 20. Endophilin-1 regulates blood-brain barrier permeability by controlling ZO-1 and occludin expression via the EGFR-ERK1/2 pathway. |
| GO:0045121 membrane raft | ISS GO_REF:0000024 | ACCEPT | Summary: EGFR localizes to membrane rafts/lipid rafts in the plasma membrane. Reason: EGFR partitioning into membrane rafts affects its signaling. |
| GO:0051117 ATPase binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: EGFR may bind to ATPases. Reason: ATPase binding is not a primary EGFR function. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868658 | ACCEPT | Summary: EGFR undergoes clathrin-mediated endocytosis and localizes to clathrin-coated vesicles. Reason: Clathrin-mediated endocytosis is a major route for EGFR internalization. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868659 | ACCEPT | Summary: EGFR undergoes clathrin-mediated endocytosis and localizes to clathrin-coated vesicles. Reason: Clathrin-mediated endocytosis is a major route for EGFR internalization. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868660 | ACCEPT | Summary: EGFR undergoes clathrin-mediated endocytosis and localizes to clathrin-coated vesicles. Reason: Clathrin-mediated endocytosis is a major route for EGFR internalization. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868661 | ACCEPT | Summary: EGFR undergoes clathrin-mediated endocytosis and localizes to clathrin-coated vesicles. Reason: Clathrin-mediated endocytosis is a major route for EGFR internalization. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8869438 | ACCEPT | Summary: EGFR undergoes clathrin-mediated endocytosis and localizes to clathrin-coated vesicles. Reason: Clathrin-mediated endocytosis is a major route for EGFR internalization. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8871193 | ACCEPT | Summary: EGFR undergoes clathrin-mediated endocytosis and localizes to clathrin-coated vesicles. Reason: Clathrin-mediated endocytosis is a major route for EGFR internalization. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8871194 | ACCEPT | Summary: EGFR undergoes clathrin-mediated endocytosis and localizes to clathrin-coated vesicles. Reason: Clathrin-mediated endocytosis is a major route for EGFR internalization. |
| GO:0005737 cytoplasm | IDA PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | ACCEPT | Summary: EGFR intracellular domain localizes to the cytoplasm. Reason: The cytoplasmic portion of EGFR containing the kinase domain is localized in the cytoplasm. Supporting Evidence: PMID:22298428 Feb 1. The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. |
| GO:0005886 plasma membrane | IDA PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. Supporting Evidence: PMID:22298428 Feb 1. The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. |
| GO:0005515 protein binding | IPI PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:22298428 Feb 1. The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1169421 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1218833 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220610 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220612 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220613 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220614 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225947 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225949 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225950 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225951 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225952 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225956 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225957 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225960 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225961 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1226012 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1226014 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1226016 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247841 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247842 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247844 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220611 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0019903 protein phosphatase binding | IPI PMID:28759036 Deficiency in VHR/DUSP3, a suppressor of focal adhesion kina... | ACCEPT | Summary: EGFR binds to protein phosphatases that regulate its phosphorylation state. Reason: EGFR is regulated by phosphatases including PTPN1, PTPN2, and PTPN12. Supporting Evidence: PMID:28759036 Jul 31. Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration. |
| GO:0010008 endosome membrane | TAS Reactome:R-HSA-9611147 | ACCEPT | Summary: EGFR localizes to endosome membranes during receptor trafficking after internalization. Reason: After ligand-induced endocytosis, EGFR is found on endosome membranes where it continues to signal. |
| GO:0045296 cadherin binding | HDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by... | KEEP AS NON CORE | Summary: EGFR binds to cadherins, linking to cell adhesion regulation. Reason: Cadherin binding represents crosstalk between EGFR and cell adhesion. Supporting Evidence: PMID:25468996 E-cadherin interactome complexity and robustness resolved by quantitative proteomics. |
| GO:0030335 positive regulation of cell migration | IMP PMID:25678558 Navigator-3, a modulator of cell migration, may act as a sup... | KEEP AS NON CORE | Summary: EGFR signaling promotes cell migration through various downstream effectors. Reason: Cell migration is a downstream cellular behavior influenced by EGFR signaling. Supporting Evidence: PMID:25678558 Navigator-3, a modulator of cell migration, may act as a suppressor of breast cancer progression. |
| GO:0005515 protein binding | IPI PMID:28479384 Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in ... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:28479384 Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer cells. |
| GO:0004713 protein tyrosine kinase activity | IMP PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. Supporting Evidence: PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary carcinogenesis. |
| GO:0005515 protein binding | IPI PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary carcinogenesis. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IMP PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary carcinogenesis. |
| GO:0032991 protein-containing complex | IDA PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | ACCEPT | Summary: EGFR forms protein complexes with signaling partners. Reason: EGFR exists in multiprotein signaling complexes. Supporting Evidence: PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary carcinogenesis. |
| GO:0033138 positive regulation of peptidyl-serine phosphorylation | IMP PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | KEEP AS NON CORE | Summary: EGFR signaling leads to downstream serine phosphorylation events. Reason: Serine phosphorylation regulation is a downstream effect of EGFR signaling cascades. Supporting Evidence: PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mammary carcinogenesis. |
| GO:0005006 epidermal growth factor receptor activity | IMP PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediated inactivation of the EGF receptor. |
| GO:1903078 positive regulation of protein localization to plasma membrane | IDA PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | KEEP AS NON CORE | Summary: EGFR signaling can regulate protein localization to plasma membrane. Reason: Downstream cellular effect. Supporting Evidence: PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediated inactivation of the EGF receptor. |
| GO:0005886 plasma membrane | IDA PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. Supporting Evidence: PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediated inactivation of the EGF receptor. |
| GO:1905208 negative regulation of cardiocyte differentiation | IMP PMID:23069713 The promotion of cardiogenic differentiation of hMSCs by tar... | KEEP AS NON CORE | Summary: EGFR signaling negatively regulates cardiocyte differentiation. Reason: Cell type-specific developmental effect. Supporting Evidence: PMID:23069713 Epub 2012 Oct 13. The promotion of cardiogenic differentiation of hMSCs by targeting epidermal growth factor receptor using microRNA-133a. |
| GO:0005768 endosome | IDA PMID:16554368 The ESCRT-III subunit hVps24 is required for degradation but... | ACCEPT | Summary: EGFR localizes to endosomes following ligand-induced internalization. EGFR continues signaling from early endosomes and is subsequently sorted for recycling or lysosomal degradation. Reason: Endosomal localization is part of normal EGFR trafficking and signaling. EGFR signals from endosomes and trafficking modulates signal duration. Supporting Evidence: PMID:16554368 Mar 22. The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor. |
| GO:0008284 positive regulation of cell population proliferation | IMP PMID:27057632 Tumor-suppressive miR-218-5p inhibits cancer cell proliferat... | KEEP AS NON CORE | Summary: EGFR signaling promotes cell proliferation through MAPK and PI3K pathways. Reason: Cell proliferation is a downstream phenotypic effect of EGFR signaling. Supporting Evidence: PMID:27057632 Tumor-suppressive miR-218-5p inhibits cancer cell proliferation and migration via EGFR in non-small cell lung cancer. |
| GO:0070374 positive regulation of ERK1 and ERK2 cascade | IMP PMID:21673316 TRPS1 targeting by miR-221/222 promotes the epithelial-to-me... | ACCEPT | Summary: EGFR positively regulates ERK1/2 cascade through RAS-RAF-MEK-ERK signaling axis. Reason: ERK1/2 activation is a core readout of EGFR signaling through the MAPK pathway. Supporting Evidence: PMID:21673316 TRPS1 targeting by miR-221/222 promotes the epithelial-to-mesenchymal transition in breast cancer. |
| GO:0030307 positive regulation of cell growth | IDA PMID:15467833 CEACAM1 modulates epidermal growth factor receptor--mediated... | KEEP AS NON CORE | Summary: EGFR signaling promotes cell growth. Reason: Cell growth regulation is a downstream effect of EGFR activation. Supporting Evidence: PMID:15467833 CEACAM1 modulates epidermal growth factor receptor--mediated cell proliferation. |
| GO:0005515 protein binding | IPI PMID:23912460 Hyperactivation of EGFR and downstream effector phospholipas... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:23912460 Aug 5. Hyperactivation of EGFR and downstream effector phospholipase D1 by oncogenic FAM83B. |
| GO:0005515 protein binding | IPI PMID:25311788 EGFR phosphorylates and inhibits lung tumor suppressor GPRC5... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25311788 EGFR phosphorylates and inhibits lung tumor suppressor GPRC5A in lung cancer. |
| GO:0005515 protein binding | IPI PMID:25666625 Epidermal growth factor receptor (EGFR) signaling requires a... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:25666625 2015 Feb 9. Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface. |
| GO:0009986 cell surface | IDA PMID:25666625 Epidermal growth factor receptor (EGFR) signaling requires a... | ACCEPT | Summary: EGFR localizes to the cell surface where it is accessible for ligand binding. Reason: Cell surface localization is consistent with EGFR function as a receptor for extracellular growth factors. Supporting Evidence: PMID:25666625 2015 Feb 9. Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface. |
| GO:0031901 early endosome membrane | IDA PMID:17714434 Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth... | ACCEPT | Summary: EGFR localizes to early endosome membranes following internalization, where it continues to signal. Reason: Early endosome membrane localization is well-documented for EGFR trafficking. Supporting Evidence: PMID:17714434 2007 Aug 20. Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation. |
| GO:0097489 multivesicular body, internal vesicle lumen | IDA PMID:17714434 Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth... | ACCEPT | Summary: EGFR is sorted into multivesicular bodies for lysosomal degradation. Reason: MVB sorting is part of EGFR downregulation pathway. Supporting Evidence: PMID:17714434 2007 Aug 20. Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth factor and chemokine receptors destined for lysosomal degradation. |
| GO:0005515 protein binding | IPI PMID:8305738 The human GRB2 and Drosophila Drk genes can functionally rep... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:8305738 The human GRB2 and Drosophila Drk genes can functionally replace the Caenorhabditis elegans cell signaling gene sem-5. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:23418353 The E3 ubiquitin ligases RNF126 and Rabring7 regulate endoso... | ACCEPT | Summary: EGFR binds to CBL E3 ubiquitin ligase, which ubiquitinates EGFR for endocytosis and degradation. Reason: CBL binding to EGFR is critical for receptor downregulation. Supporting Evidence: PMID:23418353 Feb 15. The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor. |
| GO:0010008 endosome membrane | IDA PMID:22719997 SNX12 role in endosome membrane transport. | ACCEPT | Summary: EGFR localizes to endosome membranes during receptor trafficking after internalization. Reason: After ligand-induced endocytosis, EGFR is found on endosome membranes where it continues to signal. Supporting Evidence: PMID:22719997 SNX12 role in endosome membrane transport. |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | KEEP AS NON CORE | Summary: EGFR localizes to focal adhesions during cell migration. Reason: Focal adhesion localization is associated with EGFR-mediated migration. Supporting Evidence: PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for Ξ²-Pix in negative regulation of focal adhesion maturation. |
| GO:0005515 protein binding | IPI PMID:9852145 Interaction of ZPR1 with translation elongation factor-1alph... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9852145 Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells. |
| GO:0043235 receptor complex | IDA PMID:23382219 Structural basis for endosomal trafficking of diverse transm... | ACCEPT | Summary: EGFR forms homo- and heterodimeric receptor complexes upon ligand binding, which is required for kinase activation. Reason: EGFR dimerization into receptor complexes is essential for signal transduction. EGFR forms homodimers and heterodimers with ERBB2, ERBB3, ERBB4. Supporting Evidence: PMID:23382219 Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins. |
| GO:0007611 learning or memory | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: EGFR signaling may influence learning and memory processes. Reason: High-level behavioral phenotype, represents very downstream effects. |
| GO:0071364 cellular response to epidermal growth factor stimulus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: EGFR mediates cellular responses to EGF. Reason: This describes the cellular response, not the core receptor function. |
| GO:0001934 positive regulation of protein phosphorylation | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: EGFR promotes protein phosphorylation through its kinase activity and downstream signaling. Reason: This is a general downstream effect of EGFR signaling. Supporting Evidence: PMID:20551055 Epub 2010 Jun 15. Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. |
| GO:0003682 chromatin binding | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: Nuclear EGFR has been reported to bind chromatin and regulate transcription. Reason: Nuclear EGFR has been described in some contexts, but this is not a core function of EGFR. Supporting Evidence: PMID:20551055 Epub 2010 Jun 15. Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. |
| GO:0005515 protein binding | IPI PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:20551055 Epub 2010 Jun 15. Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. |
| GO:0005634 nucleus | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: Nuclear EGFR has been described in certain contexts and may have transcriptional roles. Reason: Nuclear EGFR is documented but represents a minor, context-dependent localization rather than core EGFR function. Supporting Evidence: PMID:20551055 Epub 2010 Jun 15. Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: EGFR signaling leads to transcriptional activation of target genes. Reason: Transcriptional regulation is a downstream effect of EGFR signaling pathways. Supporting Evidence: PMID:20551055 Epub 2010 Jun 15. Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. |
| GO:0070374 positive regulation of ERK1 and ERK2 cascade | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | ACCEPT | Summary: EGFR positively regulates ERK1/2 cascade through RAS-RAF-MEK-ERK signaling axis. Reason: ERK1/2 activation is a core readout of EGFR signaling through the MAPK pathway. Supporting Evidence: PMID:20551055 Epub 2010 Jun 15. Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. |
| GO:0071392 cellular response to estradiol stimulus | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: EGFR can be activated in response to estradiol through crosstalk mechanisms. Reason: Estradiol response represents crosstalk/secondary activation, not core function. Supporting Evidence: PMID:20551055 Epub 2010 Jun 15. Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247999 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1248002 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1248655 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637764 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637765 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637766 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637770 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637792 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637794 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637795 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637796 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637798 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637800 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637801 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637806 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637808 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5638137 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250195 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306957 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306963 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306965 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177923 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177924 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177925 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177926 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177927 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177930 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177933 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177934 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177936 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177937 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177938 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177939 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177941 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177943 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177944 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177945 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182969 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182986 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182990 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182993 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182994 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183002 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183036 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183051 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183055 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183058 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183067 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183072 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183084 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183089 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963563 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963581 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963582 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212706 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212710 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212713 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2179387 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2179407 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2179415 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672965 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6785636 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6785648 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8847995 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8848005 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864105 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864125 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8866279 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867041 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867044 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867047 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867754 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867756 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868071 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868072 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868230 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868236 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868648 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868651 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868661 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8951490 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9018572 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9018573 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9625482 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9625487 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664588 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664918 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664933 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664940 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664950 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664976 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664983 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664991 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665000 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665009 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665032 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665034 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665389 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665404 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665406 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665407 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665408 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665409 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665410 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665411 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665413 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665415 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665416 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665417 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665698 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665699 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665700 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665701 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665704 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665705 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665706 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665707 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665709 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1248744 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1251923 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1251929 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005515 protein binding | IPI PMID:19509291 GAREM, a novel adaptor protein for growth factor receptor-bo... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:19509291 2009 Jun 9. GAREM, a novel adaptor protein for growth factor receptor-bound protein 2, contributes to cellular transformation through the activation of extracellular signal-regulated kinase signaling. |
| GO:0005515 protein binding | IPI PMID:18602463 Ataxin-2 associates with the endocytosis complex and affects... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:18602463 2008 Jun 15. Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking. |
| GO:0005515 protein binding | IPI PMID:10026169 Identification of Grb4/Nckbeta, a src homology 2 and 3 domai... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:10026169 Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck. |
| GO:0005515 protein binding | IPI PMID:15590694 Suppressors of cytokine signaling 4 and 5 regulate epidermal... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:15590694 2004 Dec 7. Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. Supporting Evidence: PMID:17115032 Tyrosine phosphorylation controls PCNA function through protein stability. |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:17115032 Tyrosine phosphorylation controls PCNA function through protein stability. |
| GO:0005515 protein binding | IPI PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17115032 Tyrosine phosphorylation controls PCNA function through protein stability. |
| GO:0005634 nucleus | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: Nuclear EGFR has been described in certain contexts and may have transcriptional roles. Reason: Nuclear EGFR is documented but represents a minor, context-dependent localization rather than core EGFR function. Supporting Evidence: PMID:17115032 Tyrosine phosphorylation controls PCNA function through protein stability. |
| GO:0042177 negative regulation of protein catabolic process | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: EGFR signaling can inhibit protein catabolism. Reason: Downstream effect of EGFR survival signaling. Supporting Evidence: PMID:17115032 Tyrosine phosphorylation controls PCNA function through protein stability. |
| GO:0045739 positive regulation of DNA repair | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: Nuclear EGFR has been implicated in DNA repair regulation. Reason: DNA repair regulation is a non-canonical nuclear EGFR function. Supporting Evidence: PMID:17115032 Tyrosine phosphorylation controls PCNA function through protein stability. |
| GO:0045740 positive regulation of DNA replication | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: EGFR signaling promotes DNA replication through proliferative signaling. Reason: DNA replication regulation is downstream of EGFR proliferative signaling. Supporting Evidence: PMID:17115032 Tyrosine phosphorylation controls PCNA function through protein stability. |
| GO:0019899 enzyme binding | IPI PMID:12009895 Plasma membrane phospholipid scramblase 1 is enriched in lip... | ACCEPT | Summary: EGFR binds to downstream enzymes including kinases and phosphatases. Reason: EGFR interacts with various enzymes as part of signaling. Supporting Evidence: PMID:12009895 Plasma membrane phospholipid scramblase 1 is enriched in lipid rafts and interacts with the epidermal growth factor receptor. |
| GO:0045121 membrane raft | IDA PMID:12009895 Plasma membrane phospholipid scramblase 1 is enriched in lip... | ACCEPT | Summary: EGFR localizes to membrane rafts/lipid rafts in the plasma membrane. Reason: EGFR partitioning into membrane rafts affects its signaling. Supporting Evidence: PMID:12009895 Plasma membrane phospholipid scramblase 1 is enriched in lipid rafts and interacts with the epidermal growth factor receptor. |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:18070883 A novel role of Sprouty 2 in regulating cellular apoptosis. | KEEP AS NON CORE | Summary: EGFR signaling promotes cell survival by activating anti-apoptotic pathways including PI3K-AKT. Reason: Anti-apoptotic effects are downstream consequences of EGFR-PI3K-AKT signaling, not a core function. Supporting Evidence: PMID:18070883 2007 Dec 10. A novel role of Sprouty 2 in regulating cellular apoptosis. |
| GO:0005515 protein binding | IPI PMID:17182860 Activated Cdc42-associated kinase 1 is a component of EGF re... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17182860 Dec 20. Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation. |
| GO:0005768 endosome | IDA PMID:17182860 Activated Cdc42-associated kinase 1 is a component of EGF re... | ACCEPT | Summary: EGFR localizes to endosomes following ligand-induced internalization. EGFR continues signaling from early endosomes and is subsequently sorted for recycling or lysosomal degradation. Reason: Endosomal localization is part of normal EGFR trafficking and signaling. EGFR signals from endosomes and trafficking modulates signal duration. Supporting Evidence: PMID:17182860 Dec 20. Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation. |
| GO:0004888 transmembrane signaling receptor activity | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | ACCEPT | Summary: EGFR is a transmembrane signaling receptor. Reason: This accurately describes EGFR as a transmembrane receptor. Supporting Evidence: PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. |
| GO:0007166 cell surface receptor signaling pathway | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | KEEP AS NON CORE | Summary: EGFR participates in cell surface receptor signaling. Reason: This general term is accurate but less specific than EGFR signaling pathway terms. Supporting Evidence: PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | ACCEPT | Summary: EGFR is the initiating receptor of the EGF receptor signaling pathway, binding EGF family ligands and activating downstream signaling cascades. Reason: This is the defining biological process for EGFR - it is the primary receptor that initiates this pathway. Supporting Evidence: PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. |
| GO:0008284 positive regulation of cell population proliferation | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | KEEP AS NON CORE | Summary: EGFR signaling promotes cell proliferation through MAPK and PI3K pathways. Reason: Cell proliferation is a downstream phenotypic effect of EGFR signaling. Supporting Evidence: PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. |
| GO:0090263 positive regulation of canonical Wnt signaling pathway | IMP PMID:20302655 Epidermal growth factor receptor regulates beta-catenin loca... | KEEP AS NON CORE | Summary: EGFR signaling can crosstalk with and regulate Wnt signaling. Reason: Wnt pathway crosstalk is a secondary/downstream effect of EGFR. Supporting Evidence: PMID:20302655 Epidermal growth factor receptor regulates beta-catenin location, stability, and transcriptional activity in oral cancer. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:17599051 The evolutionarily conserved EBR module of RALT/MIG6 mediate... | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. Supporting Evidence: PMID:17599051 Jun 18. The evolutionarily conserved EBR module of RALT/MIG6 mediates suppression of the EGFR catalytic activity. |
| GO:0005515 protein binding | IPI PMID:17599051 The evolutionarily conserved EBR module of RALT/MIG6 mediate... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17599051 Jun 18. The evolutionarily conserved EBR module of RALT/MIG6 mediates suppression of the EGFR catalytic activity. |
| GO:0005737 cytoplasm | IDA PMID:7588596 WT1 suppresses synthesis of the epidermal growth factor rece... | ACCEPT | Summary: EGFR intracellular domain localizes to the cytoplasm. Reason: The cytoplasmic portion of EGFR containing the kinase domain is localized in the cytoplasm. Supporting Evidence: PMID:7588596 WT1 suppresses synthesis of the epidermal growth factor receptor and induces apoptosis. |
| GO:0005515 protein binding | IPI PMID:19602593 Cetuximab/C225-induced intracellular trafficking of epiderma... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:19602593 Epub 2009 Jul 14. Cetuximab/C225-induced intracellular trafficking of epidermal growth factor receptor. |
| GO:0070435 Shc-EGFR complex | ISS GO_REF:0000024 | ACCEPT | Summary: EGFR forms a complex with SHC adaptor protein. Reason: SHC binding to phosphorylated EGFR is a key signaling event. |
| GO:0019903 protein phosphatase binding | IPI PMID:15899872 Transforming growth factor {beta} (TGF-{beta})-Smad target g... | ACCEPT | Summary: EGFR binds to protein phosphatases that regulate its phosphorylation state. Reason: EGFR is regulated by phosphatases including PTPN1, PTPN2, and PTPN12. 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:0070141 response to UV-A | IDA PMID:18483258 UVA-induced cell cycle progression is mediated by a disinteg... | KEEP AS NON CORE | Summary: EGFR can be activated by UV-A exposure. Reason: UV-A activation is a stress response, not normal physiological activation. Supporting Evidence: PMID:18483258 UVA-induced cell cycle progression is mediated by a disintegrin and metalloprotease/epidermal growth factor receptor/AKT/Cyclin D1 pathways in keratinocytes. |
| GO:0005515 protein binding | IPI PMID:17909029 The phosphoinositide kinase PIKfyve mediates epidermal growt... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:17909029 The phosphoinositide kinase PIKfyve mediates epidermal growth factor receptor trafficking to the nucleus. |
| GO:0016323 basolateral plasma membrane | IDA PMID:12646923 Segregation of receptor and ligand regulates activation of e... | ACCEPT | Summary: In polarized epithelial cells, EGFR localizes to the basolateral plasma membrane. Reason: EGFR shows polarized distribution in epithelial cells, localizing to basolateral membranes. Supporting Evidence: PMID:12646923 Segregation of receptor and ligand regulates activation of epithelial growth factor receptor. |
| GO:0005515 protein binding | IPI PMID:11279102 Sorting nexin 6, a novel SNX, interacts with the transformin... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:11279102 2001 Mar 8. Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225978 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1248677 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177922 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177942 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963586 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963589 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1977959 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-445069 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857549 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857555 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857565 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857577 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857583 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8874797 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9609689 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9610867 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9611147 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9611158 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634702 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664567 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665388 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665697 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9674531 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9851407 | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. |
| GO:0007165 signal transduction | IDA PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | ACCEPT | Summary: EGFR mediates signal transduction from extracellular growth factors to intracellular signaling cascades. Reason: Signal transduction is a core function of EGFR as a receptor tyrosine kinase. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. |
| 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: EGFR signaling promotes epithelial cell proliferation, a key downstream effect in epithelial tissues. Reason: Epithelial cell proliferation is a major physiological outcome of EGFR signaling but represents a downstream effect. Supporting Evidence: PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells overexpressing ErbB-2. |
| GO:0005515 protein binding | IPI PMID:9419975 Epiregulin binds to epidermal growth factor receptor and Erb... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:9419975 Epiregulin binds to epidermal growth factor receptor and ErbB-4 and induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-2, ErbB-3 and ErbB-4. |
| GO:0005515 protein binding | IPI PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF recep... | REMOVE | Summary: Generic 'protein binding' term provides no specific information about EGFR molecular function. Reason: Per GO curation guidelines, 'protein binding' is uninformative and should be replaced with more specific binding terms. EGFR interacts with many proteins including ligands (EGF), dimerization partners (ERBB2-4), adaptors (GRB2, SHC), and signaling molecules, but this generic term does not capture any specific binding activity. Supporting Evidence: PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma. |
| GO:0004709 MAP kinase kinase kinase activity | NAS PMID:15542601 Activation of the epidermal growth factor receptor by respir... | MARK AS OVER ANNOTATED | Summary: EGFR is not a direct MAP3K. EGFR activates the MAPK cascade but acts upstream of RAF (the actual MAP3K). Reason: EGFR is a receptor tyrosine kinase that activates RAS, which then activates RAF (the MAP3K). EGFR itself does not have MAP3K activity. Supporting Evidence: PMID:15542601 2004 Nov 12. Activation of the epidermal growth factor receptor by respiratory syncytial virus results in increased inflammation and delayed apoptosis. |
| GO:0004713 protein tyrosine kinase activity | IMP PMID:14702346 Sorting of ligand-activated epidermal growth factor receptor... | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. Supporting Evidence: PMID:14702346 2003 Dec 31. Sorting of ligand-activated epidermal growth factor receptor to lysosomes requires its actin-binding domain. |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0005634 nucleus | IDA PMID:12828935 Activation of epidermal growth factor receptor signals induc... | KEEP AS NON CORE | Summary: Nuclear EGFR has been described in certain contexts and may have transcriptional roles. Reason: Nuclear EGFR is documented but represents a minor, context-dependent localization rather than core EGFR function. Supporting Evidence: PMID:12828935 Activation of epidermal growth factor receptor signals induction of nitric oxide synthase-2 in human optic nerve head astrocytes in glaucomatous optic neuropathy. |
| GO:0005737 cytoplasm | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | ACCEPT | Summary: EGFR intracellular domain localizes to the cytoplasm. Reason: The cytoplasmic portion of EGFR containing the kinase domain is localized in the cytoplasm. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0005768 endosome | IDA PMID:14702346 Sorting of ligand-activated epidermal growth factor receptor... | ACCEPT | Summary: EGFR localizes to endosomes following ligand-induced internalization. EGFR continues signaling from early endosomes and is subsequently sorted for recycling or lysosomal degradation. Reason: Endosomal localization is part of normal EGFR trafficking and signaling. EGFR signals from endosomes and trafficking modulates signal duration. Supporting Evidence: PMID:14702346 2003 Dec 31. Sorting of ligand-activated epidermal growth factor receptor to lysosomes requires its actin-binding domain. |
| GO:0016020 membrane | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | ACCEPT | Summary: EGFR is an integral membrane protein spanning the plasma membrane with extracellular ligand-binding and intracellular kinase domains. Reason: EGFR is a type I transmembrane protein; membrane localization is fundamental to its structure and function. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0030335 positive regulation of cell migration | IMP PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | KEEP AS NON CORE | Summary: EGFR signaling promotes cell migration through various downstream effectors. Reason: Cell migration is a downstream cellular behavior influenced by EGFR signaling. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0050730 regulation of peptidyl-tyrosine phosphorylation | IMP PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | KEEP AS NON CORE | Summary: EGFR regulates tyrosine phosphorylation of substrates. Reason: While related to EGFR kinase activity, this describes regulatory outcomes. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0051015 actin filament binding | IDA PMID:14702346 Sorting of ligand-activated epidermal growth factor receptor... | KEEP AS NON CORE | Summary: EGFR has been reported to bind actin filaments. Reason: Actin binding may be involved in EGFR trafficking/localization. Supporting Evidence: PMID:14702346 2003 Dec 31. Sorting of ligand-activated epidermal growth factor receptor to lysosomes requires its actin-binding domain. |
| GO:0051205 protein insertion into membrane | TAS PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | KEEP AS NON CORE | Summary: EGFR is inserted into the membrane during biosynthesis. Reason: Describes EGFR biogenesis rather than function. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0098609 cell-cell adhesion | IMP PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | KEEP AS NON CORE | Summary: EGFR signaling influences cell-cell adhesion. Reason: Downstream cellular behavior. Supporting Evidence: PMID:12435727 2002 Nov 14. Epidermal growth factor receptor mediates increased cell proliferation, migration, and aggregation in esophageal keratinocytes in vitro and in vivo. |
| GO:0001503 ossification | NAS PMID:12925580 Mice humanised for the EGF receptor display hypomorphic phen... | KEEP AS NON CORE | Summary: EGFR signaling may influence bone formation. Reason: Developmental process in bone tissue. Supporting Evidence: PMID:12925580 Mice humanised for the EGF receptor display hypomorphic phenotypes in skin, bone and heart. |
| GO:0005615 extracellular space | NAS PMID:9103388 Expression of a truncated epidermal growth factor receptor-l... | KEEP AS NON CORE | Summary: Soluble EGFR ectodomain isoforms may be released to extracellular space. Reason: Truncated soluble EGFR isoforms exist but this is not the primary EGFR form. Supporting Evidence: PMID:9103388 Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer. |
| GO:0042327 positive regulation of phosphorylation | IDA PMID:15082764 Epidermal growth factor receptor stimulation activates the R... | KEEP AS NON CORE | Summary: EGFR promotes phosphorylation through its kinase activity. Reason: General phosphorylation regulation is downstream of EGFR kinase activity. Supporting Evidence: PMID:15082764 Epidermal growth factor receptor stimulation activates the RNA binding protein CUG-BP1 and increases expression of C/EBPbeta-LIP in mammary epithelial cells. |
| GO:0003690 double-stranded DNA binding | NAS PMID:6325948 ATP-stimulated interaction between epidermal growth factor r... | MARK AS OVER ANNOTATED | Summary: Nuclear EGFR has been reported to associate with chromatin, but direct DNA binding is controversial. Reason: While nuclear EGFR has been described, its direct DNA binding role is not well-established and may be indirect through transcription factor interactions. Supporting Evidence: PMID:6325948 ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. |
| GO:0004713 protein tyrosine kinase activity | TAS PMID:16076471 The epidermal growth factor receptors and their family of li... | ACCEPT | Summary: EGFR possesses protein tyrosine kinase activity, phosphorylating itself and downstream substrates upon activation. Reason: Protein tyrosine kinase activity is fundamental to EGFR signaling. This is the parent term of transmembrane receptor protein tyrosine kinase activity and accurately describes EGFR function. Supporting Evidence: PMID:16076471 The epidermal growth factor receptors and their family of ligands: their putative role in atherogenesis. |
| GO:0005006 epidermal growth factor receptor activity | NAS PMID:2790960 Functional independence of the epidermal growth factor recep... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:2790960 Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. |
| GO:0005006 epidermal growth factor receptor activity | NAS PMID:6325948 ATP-stimulated interaction between epidermal growth factor r... | ACCEPT | Summary: EGFR is the prototypical EGF receptor, binding EGF and related ligands to initiate signaling cascades controlling proliferation, survival, and differentiation. Reason: This is the most specific molecular function term for EGFR and is definitionally correct. Supporting Evidence: PMID:6325948 ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. |
| GO:0005886 plasma membrane | IDA PMID:15465819 Ubiquitin ligase activity of c-Cbl guides the epidermal grow... | ACCEPT | Summary: EGFR is a transmembrane receptor that localizes to the plasma membrane where it binds extracellular ligands and initiates intracellular signaling. Reason: Plasma membrane localization is essential for EGFR function as a cell surface receptor. EGFR resides at the plasma membrane to receive extracellular growth factor signals. Supporting Evidence: PMID:15465819 2004 Oct 1. Ubiquitin ligase activity of c-Cbl guides the epidermal growth factor receptor into clathrin-coated pits by two distinct modes of Eps15 recruitment. |
| GO:0018108 peptidyl-tyrosine phosphorylation | IEA | NEW | Summary: Core catalytic function of EGFR as a receptor tyrosine kinase that phosphorylates substrate proteins on tyrosine residues Reason: EGFR is a receptor tyrosine kinase that catalyzes the phosphorylation of tyrosine residues on target substrate proteins. Upon ligand binding and receptor dimerization, EGFR undergoes autophosphorylation of its C-terminal tyrosine residues, which then serve as docking sites for adaptor proteins. EGFR also phosphorylates numerous downstream substrate proteins on tyrosine residues to propagate growth factor signaling. This peptidyl-tyrosine phosphorylation activity is fundamental to EGFR's mechanism of signal transduction. Supporting Evidence: file:human/EGFR/EGFR-uniprot.txt Receptor tyrosine-protein kinase that binds ligands of the EGF family and activates several signaling cascades |
| GO:0046777 protein autophosphorylation | IEA | NEW | Summary: Essential mechanism of EGFR activation through trans-autophosphorylation of C-terminal tyrosine residues upon ligand-induced dimerization Reason: Protein autophosphorylation is the fundamental mechanism by which EGFR activates its signaling cascade. Upon EGF or other ligand binding, EGFR undergoes dimerization, which brings two kinase domains into proximity for trans-autophosphorylation. EGFR phosphorylates multiple tyrosine residues in its own C-terminal tail (including Y1068, Y1086, Y1148, Y1173), creating docking sites for SH2 and PTB domain-containing signaling proteins. This autophosphorylation is essential for EGFR signal transduction and downstream pathway activation. Supporting Evidence: file:human/EGFR/EGFR-uniprot.txt Receptor tyrosine-protein kinase that binds ligands of the EGF family and activates several signaling cascades |
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