EGFR is an ERBB-family transmembrane receptor tyrosine kinase that couples extracellular growth-factor binding to intracellular protein phosphorylation. Ligand-dependent receptor association and allosteric kinase activation create phosphorylated docking sites for signaling and trafficking proteins, supporting cell proliferation, survival and other responses in a cell-dependent manner. The full-length receptor acts at the plasma membrane and can signal after endocytosis; receptor sorting, recycling and degradation shape the duration and location of signaling. Endosomal and nuclear EGFR have additional experimentally defined signaling contexts, including regulation of AGO2 and PCNA, without acquiring their RNA-processing or DNA-repair catalytic activities. Oncogenic substitutions and deletion variants can alter activation, partner recruitment and localization. Four annotated natural products share portions of the extracellular region, but only the full-length product retains the complete transmembrane and intracellular kinase architecture; experimental constructs and cancer variants do not establish equivalent functions for the shorter natural products.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: The conserved cell-surface receptor pool is supported by the ancestral placement and independent human EGFR plasma-membrane annotations. Reason: The literal PAINT IBD at PTN001230349 (GAF line 47002) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. The conserved cell-surface receptor pool is supported by the ancestral placement and independent human EGFR plasma-membrane annotations. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: file:human/EGFR/EGFR-deep-research-falcon.md GO_REF:0000033 |
| GO:0043410 positive regulation of MAPK cascade | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: MAPK activation is a supported downstream signaling output. It is retained as contextual signaling rather than a separate molecular activity. Reason: The literal PAINT IBD at PTN000698827 (GAF line 10039) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. MAPK activation is a supported downstream signaling output. It is retained as contextual signaling rather than a separate molecular activity. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IBA GO_REF:0000033 | MODIFY | Summary: The broad ancestral receptor-kinase inference is sound. Human EGFR has experimental evidence for the more informative GO:0005006 epidermal growth factor receptor activity, which preserves the receptor role while specifying its ligand-receptor class. Reason: The literal PAINT IBD at PTN001230349 (GAF line 44187) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. The broad ancestral receptor-kinase inference is sound. Human EGFR has experimental evidence for the more informative GO:0005006 epidermal growth factor receptor activity, which preserves the receptor role while specifying its ligand-receptor class. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000033 |
| GO:0030182 neuron differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Neuronal differentiation is a developmental signaling context. Experimental neuron/photoreceptor-development descendants in fly Egfr support the inherited context; the exact-term query alone would have missed that grounding. Reason: The literal PAINT IBD at PTN000698827 (GAF line 45936) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Neuronal differentiation is a developmental signaling context. Experimental neuron/photoreceptor-development descendants in fly Egfr support the inherited context; the exact-term query alone would have missed that grounding. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0043066 negative regulation of apoptotic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Anti-apoptotic signaling is a supported cellular outcome of receptor activation, retained as contextual rather than a separate defining molecular function. Reason: The literal PAINT IBD at PTN000698827 (GAF line 20006) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Anti-apoptotic signaling is a supported cellular outcome of receptor activation, retained as contextual rather than a separate defining molecular function. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0007173 epidermal growth factor receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: The EGF receptor pathway is the defining signaling process of EGFR, with target experimental grounding as well as the conserved ancestral inference. Reason: The literal PAINT IBD at PTN000698827 (GAF line 35647) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. The EGF receptor pathway is the defining signaling process of EGFR, with target experimental grounding as well as the conserved ancestral inference. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: GO_REF:0000033 |
| GO:0050679 positive regulation of epithelial cell proliferation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Epithelial proliferation is a supported tissue-dependent response to receptor signaling; it does not define a separate EGFR molecular activity. Reason: The literal PAINT IBD at PTN000698827 (GAF line 25072) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Epithelial proliferation is a supported tissue-dependent response to receptor signaling; it does not define a separate EGFR molecular activity. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0043235 receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: Membership in signaling receptor complexes is part of EGFR receptor function. This does not imply identical ligand responsiveness of every ERBB heterodimer or natural product. Reason: The literal PAINT IBD at PTN001230349 (GAF line 31496) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Membership in signaling receptor complexes is part of EGFR receptor function. This does not imply identical ligand responsiveness of every ERBB heterodimer or natural product. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: GO_REF:0000033 |
| GO:0009925 basal plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Basal localization is a polarized-cell pool, supported by human and mouse basolateral-membrane experimental descendants. It is not a universal location across cell types or products. Reason: The literal PAINT IBD at PTN000698827 (GAF line 4108) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Basal localization is a polarized-cell pool, supported by human and mouse basolateral-membrane experimental descendants. It is not a universal location across cell types or products. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0048408 epidermal growth factor binding | IBA GO_REF:0000033 | ACCEPT | Summary: EGF recognition is an intrinsic ligand-binding component of the receptor mechanism. Direct mouse Egfr EGF-binding evidence grounds the EGFR-clade inference; a short donor list is not a propagation defect. Reason: The literal PAINT IBD at PTN002814603 (GAF line 23808) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. EGF recognition is an intrinsic ligand-binding component of the receptor mechanism. Direct mouse Egfr EGF-binding evidence grounds the EGFR-clade inference; a short donor list is not a propagation defect. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: GO_REF:0000033 |
| GO:0000165 MAPK cascade | IEA GO_REF:0000108 | ACCEPT | Summary: EGFR participates upstream in the MAPK signaling cascade. Reason: Retain the process assertion, but do not use its GO:0004709 source arm as proof that EGFR directly phosphorylates MAP kinase kinases. The current GO:0004709 definition requires that catalytic step. The owner independently read PMID:15542601 Methods and Results/Figure 4: EGFR inhibition or depletion reduces ERK phosphorylation and IL8 in human airway-cell RSV experiments, supporting upstream pathway participation rather than an EGFR-to-MAPKK catalytic assay. The current target FUNCTION also places EGFR upstream of RASβRAFβMEKβERK. A flawed specificity in the source MF premise does not make this independently supported process false. The original source arm remains unchanged. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IEA GO_REF:0000120 | MODIFY | Summary: EGFR-specific receptor activity is more informative than the receptor-kinase parent. Reason: The EC and ortholog arms support receptor tyrosine kinase chemistry; the reviewed human target identifies the EGF-responsive receptor. GO:0005006 combines ligand recognition with transmembrane signaling and has GO:0004714 among its current is_a/part_of closure. Refine at target level while preserving all original source arms; this is not a claim that each broad EC record alone specifies EGF recognition. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000120 |
| GO:0046718 symbiont entry into host cell | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: EGFR actively supports a postbinding viral-entry step in the tested HCV systems. Reason: PMID:21516087 directly examines human hepatocyte models, RNA interference and rescue, kinase inhibition, CD81βCLDN1 association and membrane fusion. These observations support participation in entry, beyond EGFR merely being necessary or contacted. The same original finds no EGFR-dependent E2-binding contribution, so the electronic GO:0001618 premise must not be taken as demonstrated viral-ligand binding. Keep the infection-context process non-core with this independent evidence and retain the original GO_REF/source identity. |
| GO:0000139 Golgi membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Golgi-membrane EGFR is a documented trafficking pool. Reason: The literal SL-0134 mapping is present in the reviewed human location record. Its accompanying note includes EGF-dependent traffic toward the nucleus through Golgi and ER, not only newly synthesized receptor transport. Preserve the positive compartment observation as a contextual trafficking pool; neither transient residence nor absence of a separate core function makes it an artifact. This consultation inspected the curated record, not the original localization figures. Supporting Evidence: GO_REF:0000044 |
| GO:0000166 nucleotide binding | IEA GO_REF:0000043 | MODIFY | Summary: ATP binding supplies the supported nucleotide specificity. Reason: The broad nucleotide keyword is compatible with the target, but the target kinase domain and ATP-binding annotation resolve the nucleotide. GO:0005524 is a current descendant of GO:0000166. Refine without implying ATP hydrolysis or an autonomous ATPase function. Proposed replacements: ATP binding Supporting Evidence: GO_REF:0000043 |
| GO:0001618 virus receptor activity | IEA GO_REF:0000043 | UNDECIDED | Summary: Virus entry evidence does not by itself resolve virus-receptor binding activity. Reason: GO:0001618 requires both combining with a virus component and mediating entry. The inspected PMID:21516087 supports a postbinding HCV entry role but reports that EGFR suppression did not affect E2 binding and that human EGFR did not confer E2 binding in the tested CHO assay. That does not prove universal absence of viral binding. Other curated HCMV entry models are available to the owner, but their underlying virus-component-binding experiments were not independently inspected in this lane. Preserve the keyword-derived assertion as unresolved rather than converting the HCV cofactor result into either a positive binding assay or a universal negative. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: The broad kinase or transferase assertion can be specified as EGFR activity. Reason: The literal InterPro, keyword, RHEA and/or ortholog arms listed in this particular source row are retained exactly. They support kinase-domain or tyrosine-phosphorylation chemistry at differing resolutions. Independent reviewed human receptor identity supports GO:0005006, which includes the receptorβs ligand-coupled tyrosine-kinase mechanism and has this original broad MF in its current closure. The refinement does not infer EGF specificity from a generic kinase domain alone or classify EGFR as a MAP kinase kinase kinase. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000002 |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | MODIFY | Summary: The broad kinase or transferase assertion can be specified as EGFR activity. Reason: The literal InterPro, keyword, RHEA and/or ortholog arms listed in this particular source row are retained exactly. They support kinase-domain or tyrosine-phosphorylation chemistry at differing resolutions. Independent reviewed human receptor identity supports GO:0005006, which includes the receptorβs ligand-coupled tyrosine-kinase mechanism and has this original broad MF in its current closure. The refinement does not infer EGF specificity from a generic kinase domain alone or classify EGFR as a MAP kinase kinase kinase. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000120 |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP binding is an integral part of the receptor kinase mechanism. Reason: The saved target carries the mapped kinase-domain and ATP-binding-site identifiers, and its ATP-dependent tyrosine-phosphorylation chemistry makes ATP binding a mechanistic component. Preserve this source-specific positive assertion; it does not require a separate autonomous binding core or imply ATPase activity. Supporting Evidence: GO_REF:0000120 |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The extracellular mapping applies to the secreted alternative product. Reason: The literal human SL-0243 statement is explicitly attached to isoform 2. GO:0005576 excludes material still attached to the cell surface, so the inherited explanation based only on the membrane receptor ectodomain is inaccurate. Retain the positive gene-level extracellular assertion as a non-core secreted-product pool, with the current isoform scope stated in prose. Do not edit the imported annotation to manufacture an isoform field or extend secretion to the full-length membrane receptor. Supporting Evidence: GO_REF:0000044 |
| GO:0005634 nucleus | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Nuclear EGFR is a curated contextual pool supported by multiple source arms. Reason: The exact current ARBA00026330 condition set 690 is satisfied by three target FunFam identifiers plus Eukaryota. Independently, the reviewed target has a nuclear-location statement with experimental literature attribution. Preserve the ARBA, mouse/Ensembl and SL-0191 arms; a current rule match is not a reconstruction of its historical training or version. Nuclear localization remains a positive context-dependent pool without assuming every product or cell state has it. Supporting Evidence: GO_REF:0000120 |
| GO:0005768 endosome | IEA GO_REF:0000044 | MODIFY | Summary: The membrane subcompartment is supported for internalized EGFR. Reason: The reviewed target records both SL-0101 endosome and SL-0100 endosome membrane, together with single-pass membrane topology. This is evidence for membrane placement, not merely whole-organelle staining. GO:0010008 lies within the endosome closure and refines the source to the receptor-containing membrane while retaining the original SL-0101 assertion. It does not require exclusive residence or exclude receptor sorting into endosomal internal membranes. Proposed replacements: endosome membrane Supporting Evidence: GO_REF:0000044 |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: ER-membrane EGFR is a documented trafficking pool. Reason: The exact SL-0097 record has experimental attribution and identifies a type-I membrane protein. Its surrounding record describes retrograde/nuclear transport as well as secretory traffic. Preserve the positive ER compartment as non-core in this integrated review; do not dismiss it as a speculative transit artifact or claim a direct experiment was read here. Supporting Evidence: GO_REF:0000044 |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: The plasma membrane is the principal ligand-responsive receptor compartment. Reason: The combined ortholog and SL-0039 mapping agrees with the experimentally attributed reviewed human location and the defining transmembrane receptor mechanism. This positive assertion is not exclusive: endosomal, nuclear and biosynthetic/retrograde pools remain separately recorded. Supporting Evidence: GO_REF:0000120 |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IEA GO_REF:0000002 | MODIFY | Summary: The EGFR signaling pathway specifies the broad receptor-kinase pathway. Reason: The mapped IPR016245 family includes EGF/ERB receptor kinases. The human target identity and ligand-responsive signaling resolve GO:0007173, a current descendant of GO:0007169. This is a target-specific refinement of an existing process, not a NEW pathway assertion or transfer of every family memberβs ligands. Proposed replacements: epidermal growth factor receptor signaling pathway Supporting Evidence: GO_REF:0000002 |
| GO:0010008 endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: EGFR is embedded in endosomal membranes during receptor traffic and signaling. Reason: The literal SL-0100 target annotation and membrane topology support this compartment directly at the curated-record level. Keep it alongside the plasma-membrane pool; endosomal localization need not be stable or exclusive to matter mechanistically. Original localization images were not inspected by this consultation. Supporting Evidence: GO_REF:0000044 |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Principal receptor-containing membranes give more useful resolution than generic membrane. Reason: The InterPro source supplies broad membrane-receptor architecture, while the independent reviewed target resolves plasma and endosome membranes as principal functional pools. Refine to these two supported compartments. This list is not an assertion of exclusive localization: the separately retained Golgi, ER and nuclear-membrane source rows preserve other positive contextual pools, and secretion is explicitly limited to an alternative product. Proposed replacements: plasma membrane endosome membrane Supporting Evidence: GO_REF:0000002 |
| GO:0016301 kinase activity | IEA GO_REF:0000120 | MODIFY | Summary: The broad kinase or transferase assertion can be specified as EGFR activity. Reason: The literal InterPro, keyword, RHEA and/or ortholog arms listed in this particular source row are retained exactly. They support kinase-domain or tyrosine-phosphorylation chemistry at differing resolutions. Independent reviewed human receptor identity supports GO:0005006, which includes the receptorβs ligand-coupled tyrosine-kinase mechanism and has this original broad MF in its current closure. The refinement does not infer EGF specificity from a generic kinase domain alone or classify EGFR as a MAP kinase kinase kinase. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000120 |
| GO:0016740 transferase activity | IEA GO_REF:0000043 | MODIFY | Summary: The broad kinase or transferase assertion can be specified as EGFR activity. Reason: The literal InterPro, keyword, RHEA and/or ortholog arms listed in this particular source row are retained exactly. They support kinase-domain or tyrosine-phosphorylation chemistry at differing resolutions. Independent reviewed human receptor identity supports GO:0005006, which includes the receptorβs ligand-coupled tyrosine-kinase mechanism and has this original broad MF in its current closure. The refinement does not infer EGF specificity from a generic kinase domain alone or classify EGFR as a MAP kinase kinase kinase. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000043 |
| GO:0031965 nuclear membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The nuclear-membrane pool remains a positive contextual localization. Reason: The literal SL-0182 record identifies membrane-associated EGFR rather than merely a generic nuclear signal. Preserve it as non-core with the curated trafficking context; do not merge the nuclear membrane and nucleoplasm or assert original figure inspection not performed here. Supporting Evidence: GO_REF:0000044 |
| GO:0043235 receptor complex | IEA GO_REF:0000117 | ACCEPT | Summary: EGFR participates in signaling receptor complexes. Reason: The current ARBA00029086 set 5 requires IPR000494, IPR000719 and Hominidae, all present in the target snapshot. The reviewed target independently describes receptor oligomerization and signaling associations. The current name is signaling receptor complex, but the machine-imported historic label is preserved. Neither the rule predicates nor this general complex term establish one fixed stoichiometry or the same assembly in every tissue. Supporting Evidence: GO_REF:0000117 |
| GO:0070374 positive regulation of ERK1 and ERK2 cascade | IEA GO_REF:0000117 | ACCEPT | Summary: Positive ERK-cascade regulation is a principal downstream branch of EGFR signaling. Reason: ARBA00085202 set 9 is literally satisfied by two target FunFam records and Catarrhini. The target FUNCTION and the inspected PMID:15542601 support receptor-dependent ERK activation. This is positive regulation of the cascade, not EGFR itself being the MAP3K catalyst. The same positive ERK claim is accepted across the rule-derived and experimental rows; the current rule match is not described as an experiment. |
| GO:0005515 protein binding | IPI PMID:10229072 Association of Nck with tyrosine-phosphorylated SLP-76 in ac... | MODIFY | Summary: The curated EGFRβGRB2 association supports binding to a signaling scaffold. Reason: The source-linked MINT record explicitly lists human EGFRβGRB2 co-immunoprecipitation, pull-down and competition-binding evidence for this PMID, despite the abstract focusing on Nck and SLP-76. Independent official GRB2 evidence documents tethering signaling components into complexes, meeting the scaffold-protein class definition. The full original Methods were unavailable; no exact experimental insert, native stoichiometry or domain contact is asserted. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | MODIFY | Summary: EGFR associates with ERBB2 in the human bronchial epithelial model. Reason: The complete source abstract reports distinct EGFR heterodimers in human immortalized bronchial epithelial derivatives, and the literal interaction record maps the exact human EGFRβERBB2 pair to anti-bait co-immunoprecipitation. The independently captured official partner record supports the protein-kinase class. This refinement characterizes the associated partner without claiming a purified interface or applying the same heterodimer composition to both cell derivatives. The original full Methods and insert sequence were unavailable. Proposed replacements: protein kinase binding 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... | MODIFY | Summary: EGFR binds the class II phosphoinositide 3-kinase PIK3C2B. Reason: The original human A431 experiments recover PI3K-C2beta with EGFR after EGF stimulation. Additional experiments combine Sf9-derived recombinant PI3K-C2beta with immunoisolated EGFR and separately map an N-terminal binding region. Phosphatidylinositol 3-kinase binding is more informative than generic binding; the lipid-kinase activity belongs to PIK3C2B, not EGFR. The full-enzyme association is distinguished from isolated domain assays. Proposed replacements: phosphatidylinositol 3-kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11896612 Use of signal specific receptor tyrosine kinase oncoproteins... | UNDECIDED | Summary: The source-specific EGFR construct underlying the GRB2 assertion remains unresolved. Reason: The available original abstract describes Tpr-Met variants carrying docking cassettes from other receptor tyrosine kinases, while the source-linked MINT record lists EGFRβGRB2 co-immunoprecipitation. The full Methods and figure details were unavailable, so the relationship between that curated EGFR pair and the engineered cassette experiments cannot be reconstructed. The positive curation is preserved without asserting a native EGFR assay or declaring the association false. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12070153 Identification of both positive and negative domains within ... | MODIFY | Summary: EGFR associates with the transcription factor STAT1. Reason: The complete abstract describes human EGFR C-terminal truncations in 293 cells and phosphopeptide competition that identifies docking sites for STAT1 and STAT3. Independent official STAT1 evidence establishes its DNA-binding transcription-factor class. Transcription-factor binding therefore captures the partner identity without assigning DNA binding to EGFR or claiming an isolated STAT1 SH2-domain assay from the unavailable full Methods. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12297049 Crystal structure of a truncated epidermal growth factor rec... | MODIFY | Summary: The EGFR extracellular fragment binds the growth factor TGF-alpha. Reason: The original abstract reports the structure of a truncated human EGFR ectodomain bound to TGF-alpha, and the literal interaction record identifies the crystallographic fragments. Growth-factor binding describes this ligand accurately. TGF-alpha is not relabeled as EGF, and the truncated complex does not establish the behavior of every full-length or soluble natural receptor product. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12297050 Crystal structure of the complex of human epidermal growth f... | MODIFY | Summary: Human EGFR binds EGF through its extracellular region. Reason: The verified abstract of PMID:12297050 reports a human EGFR extracellular-region complex containing two receptors and two EGF molecules, with ligand contacts in domains I and III. This directly supports EGF binding as the informative refinement. Only the abstract was available in the reserved-source assessment; exact construct bounds, experimental insert sequence and natural-product assignment were not recovered. The ectodomain complex is not itself an assay of intracellular kinase activation, and the imported source identity is unchanged. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12577067 A proteomics strategy to elucidate functional protein-protei... | MODIFY | Summary: Activated EGFR binds the GRB2 SH2 domain. Reason: The complete original abstract explicitly identifies a GSTβGRB2-SH2 bait and distinguishes EGFR and SHC as direct bait interactors from other proteins recovered in the complex. This supports SH2-domain binding rather than inferring a domain contact merely from the partner architecture. Full Methods were unavailable, so exact insert boundaries and preparation details are not added. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12620237 EGF activates its receptor by removing interactions that aut... | MODIFY | Summary: EGFR binds EGF in the ectodomain structure. Reason: The original abstract and the literal crystallographic interaction record identify EGF bound to an EGFR extracellular construct. EGF binding is the appropriate specific ligand-binding term. The ectodomain preparation does not itself measure transmembrane receptor signaling, kinase activity or equivalence of natural truncated products. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:14568990 Role of the pleckstrin homology domain of PLCgamma1 in its i... | MODIFY | Summary: The PLC-gamma1 comparison directly supports EGFR SH2-domain binding. Reason: The full original Methods specify human EGFR and rat PLC-gamma1 constructs. In HEK293 cells, the PLC-gamma1 double SH2 mutant loses the EGF-induced EGFR association while retaining insulin-receptor association; the study also uses CHO cells expressing human EGFR. This supports the conserved SH2-mediated interaction while preserving the imported human PLCG1 identifier and explicitly distinguishing the rat assay construct. The insulin-receptor emphasis of the title is not evidence of an EGFR misattribution. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:14679214 A novel proteomic screen for peptide-protein interactions. | MODIFY | Summary: An EGFR phosphotyrosine peptide recruits GRB2 through the established SH2 interaction. Reason: The original abstract reports selective GRB2 retrieval by a phosphorylated EGFR peptide compared with its control. The independently read GSTβGRB2-SH2 experiment in PMID12577067 directly establishes the same receptorβdomain interaction. Together they support SH2-domain binding, without claiming that this peptide screen itself tested every GRB2 domain or a full-length receptor complex. Proposed replacements: SH2 domain binding |
| GO:0005515 protein binding | IPI PMID:14966128 Structural requirements for signal transducer and activator ... | UNDECIDED | Summary: The EGFR-derived ligand underlying the STAT3 binding assertion remains unresolved. Reason: The available abstract reports direct STAT3 binding to synthetic YXXQ phosphopeptides and tests STAT3 mutations, but does not identify the EGFR-derived ligand used for the imported pair. Full operative Methods and Results were not recovered. The biochemical positive is preserved, while its precise attribution to EGFR remains undecided; absence from the abstract is not evidence of a false interaction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15225635 Identification of 14-3-3zeta as an EGF receptor interacting ... | MODIFY | Summary: EGFR binds the 14-3-3 protein YWHAZ. Reason: The complete abstract reports EGF-stimulated association with 14-3-3zeta and loss of association after an EGFR tail deletion. Literal interaction records distinguish filter-binding evidence from microscopy colocalization. The supported partner class justifies 14-3-3 protein binding without treating colocalization alone as binding or assigning an exact contact to the individually tested serines. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15282549 LRIG1 restricts growth factor signaling by enhancing recepto... | KEEP AS NON CORE | Summary: EGFR associates with the feedback regulator LRIG1. Reason: The source abstract and literal co-immunoprecipitation records support the EGFRβLRIG1 association. LRIG1 promotes receptor ubiquitylation through recruitment of other machinery; this does not make LRIG1 itself the ubiquitin ligase. The supported accessory interaction remains non-core under the project policy. The available cache contains selected article sections rather than complete operative Methods, so detailed construct identity is not reconstructed. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15345710 The leucine-rich repeat protein LRIG1 is a negative regulato... | KEEP AS NON CORE | Summary: The second LRIG1 study supports association with EGFR. Reason: The complete abstract explicitly reports complexes between LRIG1 and ErbB receptors in cotransfected 293T cells, consistent with the literal anti-tag co-immunoprecipitation record. Separate NIH3T3 functional experiments are not conflated with the association assay. LRIG1 is retained as a positive regulatory binding partner without assigning catalytic activity to it or claiming a purified binary interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβCTNND1 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβCTNND1 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official CTNND1 record supports the cytoskeletal regulatory protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15962011 Sprouty2 acts at the Cbl/CIN85 interface to inhibit epiderma... | MODIFY | Summary: EGFR associates with the ubiquitin ligase CBL. Reason: The recovered original Figure4A and Results assay Cbl association and EGFR ubiquitylation in HEK293T cells, including Sprouty2 comparisons that disrupt the interaction. Independently established CBL ligase activity supports ubiquitin-protein-ligase binding. EGFR remains the receptor substrate and binding partner, not the ubiquitin-conjugating enzyme; the Methods refer several construct details to prior work rather than authenticating every insert sequence. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16253990 Increased proliferation and altered growth factor dependence... | MODIFY | Summary: EGFR associates with the signaling scaffold GAB2. Reason: The literal source-linked anti-tag co-immunoprecipitation supports the pair. The complete abstract describes GAB2 recruitment of GRB2, SHP2 and PI3K, while official GAB2 evidence documents receptor-associated multicomponent complexes. This supports scaffold-protein binding rather than inferring an SH2 contact from domain content. The full pair Methods were unavailable, and the EGFR-associated complex is not represented as a purified binary interface. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from APBB1. Reason: Supplementary Table 1 identifies the human APBB1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to APBB1-C, APBB1-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16499958 Crystal structure of the ubiquitin binding domains of rabex-... | KEEP AS NON CORE | Summary: Ubiquitylated EGFR associates with Rabex-5/RABGEF1. Reason: The complete abstract, literal co-immunoprecipitation records and official SUBUNIT assessment identify Rabex-5 association with ubiquitylated EGFR. The study assigns ubiquitin recognition to Rabex-5 UBDs; it does not establish a receptor contact independent of conjugated ubiquitin. Nucleotide exchange and ubiquitin recognition do not by themselves establish a fitting enzyme-binding refinement, and the separately inferred ligase role is not the activity tested here. The positive association is retained without an unsupported narrower class. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16516204 Activation of ErbB2 by 2-methyl-1,4-naphthoquinone (menadion... | MODIFY | Summary: Human keratinocyte EGFR associates with the receptor tyrosine kinase ERBB2. Reason: The indexed original Results and Figure2 caption describe EGFR immunoprecipitates containing ErbB2 in HaCaT cells, including an unstimulated association and responses to EGF or menadione. Official ERBB2 evidence establishes the receptor tyrosine kinase class. The refinement uses this physical association, while the available source route is selected original Results/caption text rather than complete Methods or figure-pixel inspection. Proposed replacements: receptor tyrosine kinase binding 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... | MODIFY | Summary: The source supports EGFRβGAPDH association with a supported partner-class refinement. Reason: The complete source abstract reports EGFR immunoprecipitation from human A431 cells at multiple times after EGF stimulation and identification of associated proteins by mass spectrometry. The literal GAPDH pair is positively curated from the source with the original table/figure locators; time-dependent recovery is not interpreted as a mapped binary interface. The full original body was not recovered, so no additional pair-specific controls are claimed. GAPDH has established enzyme activity; the association does not make its metabolic chemistry an EGFR function. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16843263 HER2 kinase domain mutation results in constitutive phosphor... | MODIFY | Summary: EGFR associates with ERBB2 in the kinase-mutation study. Reason: The original abstract describes ERBB2 kinase-mutant effects on wild-type and kinase-defective EGFR, and the literal interaction records include pull-down assays with the recorded wild-type/mutant features. Receptor tyrosine kinase binding captures the independently established ERBB2 class. The cancer-associated engineered constructs are not equated with all natural ERBB2 or EGFR products. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16914641 Intersectin regulates epidermal growth factor receptor endoc... | MODIFY | Summary: The CBL-linked assertion is consistent with independently verified EGFRβCBL binding. Reason: The available abstract addresses intersectin scaffolding of CBL and CBL-dependent EGFR ubiquitylation, but does not resolve the full pair assay. The imported IPI assertion is independently corroborated by the directly inspected EGFRβCBL association in PMID15962011. Ubiquitin-protein-ligase binding captures the verified partner class without claiming that the inaccessible Methods were read or assigning CBL catalysis to EGFR. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:16954185 Advanced glycation end product (AGE) receptor 1 suppresses c... | KEEP AS NON CORE | Summary: The paper supports EGFR protein association with AGER1, with an imported partner mismatch. Reason: The original Methods and Figure6 specify human V5-tagged AGER1 in HEK293 and mouse mesangial cells, including reciprocal co-immunoprecipitation with EGFR. The paper distinguishes AGER1 from RAGE, and current official identity maps AGER1/OST48 to DDOST/P39656; the imported Q15109 instead identifies AGER/RAGE. All source fields remain unchanged. Generic binding is retained for the actual positive AGER1 assay, but this source does not justify a RAGE-based receptor-class refinement or a claim that EGFRβRAGE association is biologically impossible. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17126326 Extracellular heat shock protein 70 mediates heat stress-ind... | MODIFY | Summary: EGFR associates with the signaling receptor TLR2 during heat-stress cross-talk. Reason: The complete abstract reports TLR2/4 activation and EGFR association in human A431 cells after heat stress or added Hsp70. Official TLR2 evidence establishes the signaling-receptor class. Signaling-receptor binding is therefore justified within that context, without inferring a purified interface, direct Hsp70βEGFR binding or an EGF-driven assay from the unavailable full Methods. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | MODIFY | Summary: The EGFR and ERBB2 receptor constructs associate in the complementation assay. Reason: The original Methods specify EGFR1β679 and ERBB2 1β686 fused to complementary beta-galactosidase fragments. EGF induces their association in the C2C12 system, with expression and reciprocal-fusion controls. Signaling receptor binding describes the verified partner class. The tested ERBB2 fragment excludes its intracellular kinase domain; this experiment does not establish binding to an intact catalytically active ERBB2. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17284441 Epidermal growth factor directs sex-specific steroid signali... | MODIFY | Summary: EGFR associates with the nuclear hormone receptor ESR1 in MCF-7 cells. Reason: The indexed original Results and Figure4 report endogenous ER-alpha in EGFR immunoprecipitates and an EGFRβER-alphaβSRC complex during estrogen stimulation. The inspected Methods distinguish these co-immunoprecipitations from engineered fluorescent SRC reporters. Official ESR1 evidence establishes the nuclear-receptor class, which describes the partner even in this extranuclear assay; the refinement does not assign DNA binding to EGFR or identify a particular natural ESR1 product. Proposed replacements: nuclear receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17403676 Rin1 interacts with signal-transducing adaptor molecule (STA... | KEEP AS NON CORE | Summary: EGFR associates with RIN1 in an EGF-dependent trafficking complex. Reason: The indexed original Results describe GFP-EGFR, RIN1-V5 and HA-STAM2 coexpression in HEK293 cells followed by EGFR immunoprecipitation, with increased recovery of RIN1 and STAM2 after EGF. This supports a physical complex. The paper separately tests the RIN1 proline-rich region in STAM binding and cites prior work for RIN1 SH2-mediated receptor recognition; those are not represented as a new isolated EGFRβSH2 assay here. RIN1 nucleotide-exchange activity alone does not establish enzyme binding. The supported trafficking association remains non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17697999 Ligand-induced structural transitions in ErbB receptor extra... | UNDECIDED | Summary: The source-specific EGF association remains incompletely adjudicated. Reason: The abstract supports ligand-dependent soluble-EGFR structural work and is consistent with the imported positive. Operative Methods/Results and construct details were not recovered, so preserve the assertion with explicit uncertainty rather than infer a wrong gene or transplant another paper's assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17726113 Inhibition of the leucine-rich repeat protein LINGO-1 enhanc... | KEEP AS NON CORE | Summary: LINGO1 association negatively regulates EGFR in the studied neuronal systems. Reason: The original Results report reciprocal immunoprecipitations in cultured cells and mouse ventral-midbrain tissue, with LINGO1-blocking antibody controls. Methods distinguish a human LINGO1-Fc reagent from mouse full-length and dominant-negative Lingo1 constructs. The positive association is retained with this cross-species scope, without equating every assay to a human native complex or inferring a purified binary interface. LINGO1 is a regulatory component of a receptor complex; no narrower binding class is assigned from the coreceptor label alone. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18046415 Inhibition of the EGF receptor by binding of MIG6 to an acti... | KEEP AS NON CORE | Summary: EGFR binds the feedback inhibitor MIG6/ERRFI1. Reason: The original directly examines MIG6 fragments bound to an EGFR kinase-domain construct, quantitative binding and inhibitory mutations, with cellular full-length MIG6 comparisons. MIG6 blocks the activating kinase-dimer interface rather than acting as a kinase itself. This well-supported inhibitory association remains non-core; the fragment structure is not treated as an assay of every natural EGFR or MIG6 product. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18273061 Structural basis for a novel intrapeptidyl H-bond and revers... | MODIFY | Summary: EGFR binds the ubiquitin ligase CBL through its receptor-recognition module. Reason: The original combines an EGFR1063β1075 phosphopeptideβCBL TKB structure with binding measurements and full-length CBL mutant co-immunoprecipitation in 293T cells. The full-protein association and independently established CBL ligase class support ubiquitin-protein-ligase binding. The isolated TKB preparation is not described as a catalytically complete ligase, and EGFR is not assigned CBL ubiquitination chemistry. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18455122 Survival of cancer cells is maintained by EGFR independent o... | MODIFY | Summary: EGFR associates with the transmembrane glucose transporter SLC5A1/SGLT1. Reason: The original reports human SGLT1 cDNA and EGFRβSGLT1 co-immunoprecipitation, including wild-type versus kinase-impaired receptor and extracellular/transmembrane versus intracellular receptor constructs. Literal interaction records retain the human identities and mapped receptor region. Transmembrane-transporter binding captures SGLT1 class without assigning glucose transport to EGFR. The kinase-independent stability effect and cellular association do not establish a purified interface or natural truncated-product equivalence. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18542056 LRIG1 negatively regulates the oncogenic EGF receptor mutant... | KEEP AS NON CORE | Summary: The oncogenic EGFRvIII receptor associates with LRIG1. Reason: The original Figure1 and Methods recover transfected EGFRvIII with endogenous LRIG1 in HEK293T cells, with FGFR comparisons. The source feature records the EGFRvIII deletion. This positive association is retained at that engineered cancer-receptor scope. The study finds CBL-independent LRIG1-mediated destabilization in its ligand-independent conditions; LRIG1 is not itself assigned ubiquitin-ligase activity or a universally CBL-dependent mechanism. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18776048 Comparisons of tyrosine phosphorylated proteins in cells exp... | KEEP AS NON CORE | Summary: MIG6/ERRFI1 binding is supported independently of the phosphorylation-screen readout. Reason: This paper measures proteins in phosphotyrosine immunoprecipitates and validates MIG6 tyrosine phosphorylation with MIG6-specific immunoprecipitation; those measurements alone do not establish an EGFRβMIG6 pair. The original explicitly cites the independently inspected MIG6βEGFR structural and binding study PMID18046415, which supports the same positive association. Generic binding is therefore retained as non-core, with direct binding attributed to that corroborating study rather than inferred from correlated phosphorylation. |
| GO:0005515 protein binding | IPI PMID:18824549 Acidic mammalian chitinase is secreted via an ADAM17/epiderm... | MODIFY | Summary: EGFR associates with the active chitinase CHIA/AMCase. Reason: The original Methods specify human full-length AMCase and EGFR in A549 cells, and reciprocal immunoprecipitation shows their association. The study separately verifies AMCase chitinase bioactivity. Enzyme binding accurately describes the catalytic partner; the chitin-hydrolysis activity belongs to AMCase, not EGFR. Regulation of AMCase secretion and inflammatory outputs is distinct from the binding result. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | MODIFY | Summary: An EGFR phosphopeptide is recognized by the protein phosphatase PTPRC/CD45. Reason: The original comparative phosphatase assay and literal interaction record identify the PTPRC622β1238 preparation acting on EGFR1066β1076 phosphorylated at1069. Protein-phosphatase binding captures this substrate-recognition association while retaining its peptide and catalytic-domain scope. It does not establish a native full-length EGFRβCD45 membrane complex or assign phosphatase activity to EGFR. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19172738 Phosphorylation-dependent binding of 14-3-3 terminates signa... | MODIFY | Summary: EGFR associates with the signaling scaffold GAB2. Reason: The original MCF-10A experiments recover EGFR with HA-tagged GAB2 and compare feedback-site mutants. The source explicitly describes recruitment through a GRB2 bridge, with GAB2 assembling SHP2, PI3K and other signaling components. Scaffold-protein binding therefore captures the partner function while retaining an indirect/co-complex mechanism. Mouse GAB2 reagents listed separately in Methods are not conflated with all other constructs, and no exact natural isoform is assigned. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19650109 Flow cytometric in situ proximity ligation analyses of prote... | MODIFY | Summary: EGFR associates with the protein kinase ERBB2. Reason: This source measures EGFRβHER2 proximity by in situ PLA in unmodified cultured cells; PLA alone does not resolve a direct interface. Independently read reciprocal co-immunoprecipitation establishes the same receptor association, and the official P04626 record grounds the kinase class. The refinement therefore uses corroborated physical association, not proximity alone or transferred ERBB2 catalytic activity. Proposed replacements: protein kinase binding |
| GO:0005515 protein binding | IPI PMID:19798056 Participation of Tom1L1 in EGF-stimulated endocytosis of EGF... | KEEP AS NON CORE | Summary: EGFR associates with the endocytic adaptor TOM1L1. Reason: The original Results show transient co-immunoprecipitation of endogenous and tagged TOM1L1 with activated EGFR in A431 cells. GRB2/SHC depletion and TOM1L1 mutants support bridging through a multiprotein complex, and separate assays map TOM1L1 binding to clathrin. The supported endocytic association remains non-core without representing it as purified direct EGFRβTOM1L1 binding or assigning a signaling-scaffold class solely from the adaptor label. Full Methods were delegated to the supplement and were not recovered here. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβAIP association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβAIP record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. AIP is a receptor-associated regulator; its name and co-chaperone association do not by themselves establish the client-binding property required for a chaperone-class refinement. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20153921 EGFR and EGFRvIII interact with PUMA to inhibit mitochondria... | KEEP AS NON CORE | Summary: EGFR and EGFRvIII associate with the proapoptotic protein PUMA/BBC3. Reason: The original examines human glioma cells and xenograft-derived material, using EGFR immunoprecipitation with IgG controls and reporting reciprocal PUMA immunoprecipitation. The association is present under basal conditions and persists during the tested apoptotic stress or EGFR inhibition. The positive regulatory association remains non-core. PUMA membership in the BCL2 family does not establish a specific BH-domain contact, and downstream apoptosis phenotypes are not substituted for the physical assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20308550 The phosphatase and tensin homolog regulates epidermal growt... | MODIFY | Summary: EGFR recruits the ubiquitin ligase CBL in the PTEN-feedback study. Reason: Original Figure4D and Methods directly distinguish non-denaturing EGFRβCBL co-immunoprecipitation in A431 cells from denaturing assays of receptor ubiquitination. PTEN knockdown shortens complex persistence rather than eliminating the initial recruitment. The independently established CBL ligase class supports ubiquitin-protein-ligase binding, without transferring its catalytic activity to EGFR or conflating human A431 assays with the separate mouse fibroblast experiments. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20403327 TRP channel regulates EGFR signaling in hair morphogenesis a... | MODIFY | Summary: EGFR associates with the transmembrane cation channel TRPV3. Reason: The original reports cellular co-immunoprecipitation in a heterologous system and corroborating association in mouse skin. Literal records identify human EGFR with mouse TRPV3-GFP; native mouse keratinocyte and human keratinocyte signaling experiments remain separate. Transmembrane-transporter binding describes the measured channel partner, without assigning channel activity to EGFR or treating the co-complex result as proof of a purified binary contact. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | MODIFY | Summary: GRB2 association supports binding to a signaling scaffold. Reason: The EGFRvIIIβGRB2 association is positive. Independent official GRB2 evidence describes tethering receptor-associated signaling components; the refinement uses that class, without asserting an SH2 contact. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20562913 Differential roles of ERK and Akt pathways in regulation of ... | MODIFY | Summary: The CBL assertion is consistent with independently measured EGFRβCBL binding. Reason: The available abstract describes EGFR trafficking and ubiquitination in human DU145 and PC3 cells, but the source-specific CBL panel was not recovered. The imported positive IPI assertion is independently supported by the directly inspected EGFRβCBL co-immunoprecipitation in PMID20308550. The verified ligase partner supports the narrower binding term, with the original paper access gap stated rather than filled by assumed Methods. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:20624308 EGFR/Met association regulates EGFR TKI resistance in breast... | MODIFY | Summary: MET association supports receptor tyrosine kinase binding. Reason: The reciprocal association and independently verified human MET class justify the term; neither proves that EGFR itself gains MET-specific chemistry. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20935677 A positive feedback loop of ER-Ξ±36/EGFR promotes malignant g... | MODIFY | Summary: EGFR associates with the ER-alpha36 hormone-receptor product. Reason: Preserve partner P03372-4. Its estrogen-receptor role supports hormone receptor binding; the source does not support assigning nuclear-receptor transcriptional activity to this product. Proposed replacements: hormone receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21203579 HER2 phosphorylation is maintained by a PKB negative feedbac... | MODIFY | Summary: EGFR associates with ERBB2 in the trastuzumab feedback experiments. Reason: The original and its correction report EGFRβHER2 co-immunoprecipitation in BT474 cells using the antibody/streptavidin methods described for Figure2A. Correction PMID26949965 removes unavailable or misassigned panels elsewhere and clarifies splices and shared controls; its revised Figure2A and Results retain this association. Receptor-tyrosine-kinase binding is supported at this cellular drug-treatment scope, without treating the correction as a blanket validation of every original panel. Proposed replacements: receptor tyrosine kinase binding |
| GO:0005515 protein binding | IPI PMID:21258405 Galectin-3 regulates MUC1 and EGFR cellular distribution and... | KEEP AS NON CORE | Summary: EGFR associates with MUC1 in pancreatic cancer cells. Reason: The complete abstract and the recovered institutional original Figure3 caption describe MUC1βEGFR immunoprecipitation and its response to galectin-3 depletion and EGF. This supports the positive association, while the accessible original route is selected figure and Results text rather than complete Methods. MUC1 is not reclassified as an enzyme or transcription factor from its downstream signaling effects; the accessory interaction remains non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21266349 EGFR nuclear translocation modulates DNA repair following ci... | MODIFY | Summary: EGFR associates with the protein kinase DNA-PKcs after genotoxic treatment. Reason: The original uses EGFR-transfected NIH3T3 mouse fibroblasts and reports reciprocal co-immunoprecipitation after cisplatin or irradiation, independently of its microscopy and proximity-ligation readouts. The literal source pair identifies human EGFR and mouse PRKDC. Protein-kinase binding captures the partner class, with wild-type and mutant comparisons retained as engineered-construct evidence. DNA repair chemistry and DNA-PK catalytic activity are not assigned to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | MODIFY | Summary: The reported HER2 association supports receptor tyrosine kinase binding. Reason: The SKBR3 EGFRβHER2 result supports the association despite its data-not-shown limit. Official P04626 verifies the receptor tyrosine kinase class. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21278788 Translationally controlled tumor protein induces human breas... | UNDECIDED | Summary: The SRC pair cannot be adjudicated from the available abstract. Reason: Src activation and EGFR phosphorylation do not independently resolve the imported association. Pair-specific original evidence was not recovered. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21349850 MAPK scaffold IQGAP1 binds the EGF receptor and modulates it... | MODIFY | Summary: EGFR binds the signaling scaffold IQGAP1. Reason: The original combines direct pull-downs using recombinant EGFR kinase or intracellular domains and IQGAP1 preparations with native A431 co-immunoprecipitation. The IQ region contributes to receptor recognition, while IQGAP1 organizes MAPK-pathway proteins; scaffold-protein binding captures the partner role without treating its GAP-like name as catalytic activity. Human receptor fragments produced in insect cells and bacterial IQGAP1 preparations are distinct from the native-cell experiment. The paper and curated record use slightly different deletion coordinates, which are not silently harmonized. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21376233 Activation of multiple proto-oncogenic tyrosine kinases in b... | MODIFY | Summary: EGFR associates with the protein phosphatase PTPN12. Reason: The primary study reports EGFRβPTPN12 bimolecular fluorescence complementation in human mammary epithelial cells. Independent official evidence establishes PTPN12 protein-tyrosine-phosphatase activity, supporting the partner-class refinement without assigning that activity to EGFR. The enhanced association of a C231S substrate-trapping mutant is demonstrated for HER2 and is not represented as an EGFR-specific substrate-trapping result. The complementation assay does not establish a purified binary interface. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21439278 Engineered epidermal growth factor mutants with faster bindi... | MODIFY | Summary: Direct EGF binding supports the ligand-specific term. Reason: Wild-type EGF is an actual SPR and cell-binding comparator. Retain its human receptor evidence separately from affinity-engineered EGF variants and murine receptor assays. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | MODIFY | Summary: EGFR associates with the signaling scaffold GRB2. Reason: The recovered original Methods specify human GRB2 cloned with a 3xFLAG tag, affinity purification and targeted proteomic measurements of the EGF-responsive network. The EGFRβGRB2 association is measured over time. Independently established GRB2 tethering of receptor-associated signaling components supports scaffold-protein binding. The refinement does not infer an experimentally mapped SH2 contact from network membership, nor equivalence of all natural GRB2 products. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21822280 Simultaneous visualization of the extracellular and cytoplas... | MODIFY | Summary: EGF binding is supported in the human receptor truncation experiment. Reason: The purified EGF-bound EGFR-delta998 complex supports ligand-specific binding. Preserve the engineered tail deletion and paper-coordinate scope instead of calling this an intact natural-product assay. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21951318 Ligand-dependent differences in estrogen receptor beta-inter... | MODIFY | Summary: EGFR associates with the nuclear hormone receptor ESR2/ER-beta. Reason: The original distinguishes an initial recombinant human FLAG-ER-beta1 assay from endogenous ER-beta immunoprecipitations in lung cancer cell lines. EGFR recovery varies with cell line and ligand conditions. The verified nuclear-receptor class supports the binding refinement even for extranuclear complexes, without assigning DNA binding to EGFR or treating the observed association as universal across tissues or ESR2 products. Proposed replacements: nuclear receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22411794 Hypoxia promotes ligand-independent EGF receptor signaling v... | KEEP AS NON CORE | Summary: EGFR associates with caveolin-1 in the studied renal carcinoma cells. Reason: Original Figure4C and Results recover EGFR with CAV1 in serum-starved 786-O cells and show reduced association after EGF. These co-immunoprecipitations are distinct from receptor crosslinking, caveolar localization and CAV1-depletion phenotypes. CAV1 contributes membrane architecture and recruits multiple proteins, but the available evidence does not resolve a more specific signaling-scaffold or domain-binding assertion for this pair. The positive caveolar association remains non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22439932 NKX2-1/TITF1/TTF-1-Induced ROR1 is required to sustain EGFR ... | MODIFY | Summary: EGFR associates with the receptor tyrosine kinase ERBB3. Reason: The verified abstract explicitly describes ROR1-dependent maintenance of the EGFRβERBB3 association, and literal curated records identify human receptor co-immunoprecipitations. The operative full paper was not recovered; construct details remain attributed to those records rather than to a direct Methods read. Current official ERBB3 evidence documents residual catalytic activity despite impaired kinase residues, supporting receptor-tyrosine-kinase binding without claiming ERBB3 has ERBB2-like catalytic capacity. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22939624 Quantitative analysis of HSP90-client interactions reveals p... | MODIFY | Summary: A weak EGFR association with HSP90-beta supports chaperone binding. Reason: The quantitative LUMIER screen classifies EGFR as a nonclient, but the independently inspected supplemental FigureS1A shows a very weak long-exposure HSP90-beta signal in the EGFR anti-FLAG immunoprecipitate. This agrees with the original statement that two screened nonclients give extremely weak co-immunoprecipitation signals and with the curated FigureS1a record. Supplemental Methods identify human ORFeome-derived tagged kinases in 293T cells, with CDC37 and EGFP controls. The refinement captures the verified chaperone partner while retaining the weak, assay-dependent association; it does not make mature EGFR a strong constitutive HSP90 client. Proposed replacements: protein-folding chaperone binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23178489 The role of insulin-like growth factor binding protein-3 in ... | KEEP AS NON CORE | Summary: EGFR associates with IGFBP3 in the reported DNA-damage response complexes. Reason: Recovered original Results and Methods distinguish anti-IGFBP3 Fab immunoprecipitation with control beads from proximity-ligation measurements. EGFR and DNA-PKcs occur in the recovered complexes, with cytoplasmic and nuclear fraction controls. This supports a physical association beyond proximity alone. IGFBP3 regulates growth-factor availability and has additional signaling functions, but it is not itself assigned growth-factor or catalytic activity; the generic association remains non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23178716 SnoN/SkiL expression is modulated via arsenic trioxide-induc... | MODIFY | Summary: EGFR associates with SHC1 in a receptorβadaptor signaling complex. Reason: The original anti-EGFR and anti-SHC immunoprecipitations in HEY ovarian carcinoma cells detect p66ShcA and GRB2 in receptor-associated complexes after EGF or arsenic trioxide treatment, with different kinetics. The authors could not resolve p46/p52ShcA because they comigrated with IgG. Scaffold-protein binding captures assembly of the measured receptorβSHCβGRB2 signaling complex without transferring the p46/p52 Ras-activation mechanism to p66 or assigning a specific natural product from band size alone. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23273428 Insights into the aberrant activity of mutant EGFR kinase do... | KEEP AS NON CORE | Summary: An engineered EGFR kinase domain binds a MIG6 fragment. Reason: The original abstract describes mutant kinase-domain structures, while the primary deposition 4I21 explicitly contains human EGFR695β1022 bearing L858R/T790M and human MIG6/ERRFI1 residues315β374, with expression-derived terminal residues. Its biological assemblies each contain one receptor fragment and one MIG6 fragment. This directly supports the inhibitor-binding association at the deposited construct scope. The full operative article was not recovered, and the structure does not establish functional equivalence of natural EGFR products. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | UNDECIDED | Summary: The source establishes EGFRβHCK proximity, with physical binding unresolved. Reason: The recovered original and literal interaction record identify proximity-ligation measurements for this pair in liver cancer cells. The paper validates a broader network and functionally studies other pairs, but no pair-specific orthogonal binding assay was established for EGFRβHCK in the inspected evidence. HCK tyrosine-kinase identity is secure; uncertainty concerns whether this source supports physical binding rather than proximity, so a kinase-binding refinement is not asserted. The positive proximity observation is preserved. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | MODIFY | Summary: EGFR associates with ERBB2 with corroboration beyond proximity ligation. Reason: The original study visualizes receptor proximity by multiplex proximity ligation in cell systems and human breast tumor tissue. Its own discussion distinguishes proximity from direct binding and notes possible chance proximity at high abundance. The separately read EGFR TAP/co-IP study provides physical-association evidence for the exact ERBB2 partner. Together with the verified protein-kinase class, this supports the refinement while retaining the distinct assays and mutant/tumor contexts; no purified interface is claimed. Proposed replacements: protein kinase binding |
| GO:0005515 protein binding | IPI PMID:23520446 Protein phosphorylation profiling using an in situ proximity... | MODIFY | Summary: EGFR associates with the protein kinase AURKA. Reason: The original distinguishes a human protein-array hit for L861Q EGFR from co-immunoprecipitation of wild-type and mutant receptors with wild-type or kinase-impaired AURKA in HEK293T cells. Proximity-ligation observations in lung cancer cells are separate corroborating context. The independently verified AURKA kinase class supports protein-kinase binding without attributing AURKA catalysis to EGFR or deriving a precise phosphotransfer mechanism from inhibitor effects. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23597562 Inhibition of tumor angiogenesis and growth by a small-molec... | MODIFY | Summary: The ligand-competition control supports EGF binding. Reason: Table S2 directly identifies the human EGF receptor and EGF competitor. Its negative drug-inhibition entry does not negate the underlying ligand binding; the FGFR-focused title is not exclusion evidence. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23636329 EGFR modulates microRNA maturation in response to hypoxia th... | MODIFY | Summary: EGFR associates with the catalytic RNA-silencing protein AGO2. Reason: The original main Results report co-immunoprecipitation and pull-down corroboration of the EGFRβAGO2 interaction, then distinguish split-YFP complementation, hypoxic enhancement, RNase resistance and endosomal localization. Official AGO2 evidence establishes RNA endonuclease activity, supporting enzyme binding. RNA cleavage and miRNA processing remain AGO2 functions rather than EGFR chemistry. Supplemental Methods and detailed construct-boundary panels were not recovered here, so the main-text domain summary is not treated as an authenticated insert sequence. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23764002 Epidermal growth factor receptor potentiates MCM7-mediated D... | MODIFY | Summary: EGFR associates with the non-receptor tyrosine kinase LYN. Reason: The original reports reciprocal EGFRβLYN co-immunoprecipitations in A431 cells. Both p56 and p53 LYN associate, while EGF preferentially enhances p56 recruitment; the separately measured EGFR phosphorylation of p56 Y32 is not available to p53, which lacks that N-terminal segment. The binding refinement reflects LYN class without assigning its downstream MCM7 phosphorylation to EGFR or making all LYN products functionally equivalent. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23799367 Threshold-controlled ubiquitination of the EGFR directs rece... | MODIFY | Summary: EGFR recruits the ubiquitin ligase CBL. Reason: The original distinguishes non-denaturing receptorβCBL co-immunoprecipitation from denaturing receptor-modification assays. Purified receptor-tail ubiquitination experiments separately include CBL, E1/E2 and GRB2. The physical association and established CBL ligase identity support ubiquitin-protein-ligase binding; receptor-tail participation does not make EGFR the ubiquitin-transfer enzyme. Human-cell assays and human EGFR constructs expressed in NR6 cells retain their distinct host contexts. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | MODIFY | Summary: EGFR associates with ERBB2 in the tested lung-cancer cell context. Reason: The original Calu-3 experiments recover EGFR together with MET, ERBB2 and ERBB3 by coimmunoprecipitation. The independently captured official partner record establishes the protein-kinase class. The refinement describes the binding partner, not transfer of its catalytic activity to EGFR. Cellular inhibitor dependencies are not substituted for a purified binary contact or direct cross-phosphorylation assay. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24034250 EGFR-mediated Beclin 1 phosphorylation in autophagy suppress... | KEEP AS NON CORE | Summary: EGFR associates with BECN1 in the studied autophagy-regulatory complex. Reason: The original Results and curated co-immunoprecipitation records support EGFRβBECN1 association and examine changes with BECN1 tyrosine mutants and defined fragments. This positive association is retained. BECN1 is a regulatory component of autophagy complexes; the inspected evidence does not establish that it is itself a catalytic enzyme or identify a more informative binding class for this pair. The recovered article content is incomplete, so the record does not claim a fully reconstructed purified interface or equivalent behavior of all natural products. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24076656 Endophilin, Lamellipodin, and Mena cooperate to regulate F-a... | KEEP AS NON CORE | Summary: EGFR co-immunoprecipitates with lamellipodin/RAPH1. Reason: The original reports tagged EGFRβRAPH1 recovery in HEK293 cells and reciprocal endogenous co-immunoprecipitation in A431 and HeLa cells with control immunoglobulin. These are positive association data. Direct binding of lamellipodin motifs to endophilin SH3 domains is a separate molecular pair and does not establish EGFR SH3-domain binding. The receptor association is retained without transferring lamellipodinβs actin-regulatory or endocytic activities to EGFR or asserting a purified native binary interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24135280 EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 a... | MODIFY | Summary: EGFR associates with the DNA-binding transcription factor STAT3. Reason: The original nuclear STAT3 immunoprecipitation detects EGFR in human glioma-cell experiments involving coexpressed wild-type receptor and EGFRvIII; EGF changes the composition of these nuclear complexes, and control immunoglobulin is negative. STAT3βs independently established transcription-factor identity supports the partner-class refinement. The assay does not assign DNA-binding transcription-factor activity to EGFR, prove a purified binary interface, or establish equivalent behavior of natural EGFR products. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβCTNND1 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official CTNND1 record supports the cytoskeletal regulatory protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24557338 Characterisation of HER heterodimers in breast cancer using ... | UNDECIDED | Summary: The source-specific EGFRβHER2 binding assertion remains unresolved beyond proximity. Reason: The authentic abstract describes measurement of HER-family heterodimers using proximity ligation in tumor tissue microarrays, and the literal pair record identifies that method. This is positive proximity evidence, but the operative original and any pair-specific orthogonal association experiment were not recovered. HER2βs receptor-kinase identity is secure; the unresolved issue is the association evidence in this particular citation. The record is not removed and does not assert that EGFR and HER2 cannot interact. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PIK3R2 association supports phosphatidylinositol 3-kinase regulatory subunit binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row10 PIK3R2 (WT/background 1,18; L858R/background 3,25). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PIK3R2 is the p85 beta regulatory subunit of PI3K; the catalytic reaction belongs to its associated p110 subunit. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24780295 Importance of EGFR/ERCC1 interaction following radiation-ind... | KEEP AS NON CORE | Summary: EGFR associates with ERCC1 in the studied DNA-damage context. Reason: The verified abstract reports mass-spectrometric identification followed by biochemical validation and proximity ligation; the curated pair records separately identify co-immunoprecipitation in Figure 2A/B. Retain this positive association with the irradiation and DNA-repair context. ERCC1 is the noncatalytic partner of the XPFβERCC1 nuclease, so nuclease or generic enzyme binding is not inferred simply from complex membership. Full operative Methods were not recovered, and a purified binary interface or natural-product equivalence is not claimed. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24947832 Differential protein-protein interactions of LRRK1 and LRRK2... | MODIFY | Summary: EGFR associates with the protein kinase LRRK1. Reason: The original protein-array screen is followed by tagged LRRK1βEGFR co-immunoprecipitation in human HEK293 cells, with the separate LRRK2 comparison retained. Independently verified LRRK1 kinase activity supports protein kinase binding as a partner-class refinement. The association does not make EGFR a catalyst of LRRK1βs reaction, establish a kinase-domain contact, or authenticate every experimental insert as a particular natural product. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | MODIFY | Summary: The LUMIER screen supports EGFR association with the enzyme FKBP5. Reason: The exact IntAct record links the human EGFRβFKBP5 pair to Supplementary Table S1 and a C-terminally tagged LUMIER assay in human 293T cells. It records a receptor mutation at positions 770β771. The main original explains anti-FLAG capture of bait and Renilla-tagged prey, expression filtering and interaction-score thresholds. The independently captured FKBP5 record establishes peptidyl-prolyl isomerase activity, supporting enzyme binding without claiming FKBP5 chemistry as an EGFR function or an untested endogenous complex. The full supplementary insert sequence was not recovered. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25136068 Mycoplasma hyorhinis infection promotes NF-ΞΊB-dependent migr... | MODIFY | Summary: EGFR associates with phosphorylated ANXA2 in the infection-associated complex. Reason: PMID25136068 Results and Figure6D explicitly report ANXA2 and phospho-Tyr23 ANXA2 recovery with EGFR. GO:0051219 describes binding to a phosphorylated protein and fits this observation. Preserve the human gastric-cell and infection context; the assay does not establish direct recognition of the phosphate, a binary interface, or calcium dependence. Recombinant p37βANXA2 binding is a different pair. Proposed replacements: phosphoprotein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The source supports EGFRβEGF association with a supported partner-class refinement. Reason: The source abstract and exact curated pair describe endogenous proximity ligation in human HeLa cells. A positive PLA signal establishes close proximity under that assay and alone does not map a direct binding interface. The independently verified primary abstract reports the EGFβEGFR ectodomain complex; only its abstract-level access is claimed. The combined evidence supports epidermal growth factor binding while the PLA and corroborating assay contexts remain separate. The original PLA Methods were unavailable after the publisher access failure; no antibody specificity control or full-paper result is invented. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: epidermal growth factor binding |
| GO:0005515 protein binding | IPI PMID:25353163 Soluble LRIG2 ectodomain is released from glioblastoma cells... | KEEP AS NON CORE | Summary: EGFR associates with LRIG2 and its released extracellular region. Reason: The original reports co-immunoprecipitation of EGFR with full-length LRIG2 and an LRIG2 extracellular construct in human glioblastoma cells, with separate evidence for release of extracellular LRIG2. These are positive associations. Proliferation and receptor-signaling effects do not by themselves establish a growth-factor or receptor molecular-function class for LRIG2. Retain generic binding with the cellular and construct limits; no purified binary binding assay or isoform equivalence is inferred. 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... | KEEP AS NON CORE | Summary: Retain the mouse Rubcn association with its exact experimental scope. Reason: The positive original supports association despite a contradictory IntAct comment. Keep the mouse partner identity; human host cells do not convert the construct into human RUBCN. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25796184 PEA-15 facilitates EGFR dephosphorylation via ERK sequestrat... | UNDECIDED | Summary: The source-specific EGFRβPTP1B physical-binding assertion is unresolved. Reason: The recovered PMID25796184 original supports endogenous EGFR/PTP1B colocalization and PTP1B-dependent dephosphorylation after PEA-15 expression. Its PLA measures STIM1/PIP2, so it cannot validate the different EGFR/PTP1B pair. No separate physical-association assay for this pair was verified in the inspected source scope or bounded IntAct capture. Preserve the imported positive without asserting absence of binding, curator error, or importing another paperβs assay. The partner phosphatase class is established; the uncertainty is the association evidence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25873175 AXL mediates resistance to PI3KΞ± inhibition by activating th... | MODIFY | Summary: EGFRβAXL coassociation supports receptor tyrosine kinase binding. Reason: PMID25873175 Figure4H and Methods document anti-EGFR co-IP of AXL in human SCC cells; Figure4I PLA is corroborating proximity evidence. Current P30530 identity/function independently establishes AXL as a receptor tyrosine kinase. This supports the class-specific binding term without claiming a purified binary interface or assigning AXL kinase activity to EGFR. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25970784 PTPRG suppresses tumor growth and invasion via inhibition of... | MODIFY | Summary: EGFR associates with the protein tyrosine phosphatase PTPRG. Reason: PMID25970784 Figure2A, Results and CoIP Methods show reciprocal EGFR/PTPRG recovery with IgG controls in the HONE1 context. Official P23470 FUNCTION independently establishes phosphatase activity. The class refinement preserves the association and expression-system limits; it neither requires a purified interface nor assigns phosphatase activity to EGFR. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26005835 RasGRP1 opposes proliferative EGFR-SOS1-Ras signals and rest... | KEEP AS NON CORE | Summary: Retain the SOS1-containing signaling-complex association as non-core. Reason: PMID26005835 Figure7f and Methods show SOS1 co-IP of phospho-EGFR and GRB2 in EGF-stimulated human HCT15 cells. This positive complex association is retained under the projectβs scoped generic-binding policy. The inspected evidence does not establish a more informative exact binding class: SOS1 GEF activity alone is not catalytic enzyme evidence, and a GRB2-mediated complex does not make SOS1 a scaffold or establish direct binary contact. The bounded term search is not a claim that no suitable term can exist. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26280537 Secreted and O-GlcNAcylated MIF binds to the human EGF recep... | MODIFY | Summary: EGF binding is the positive ligand control in the MIF study. Reason: The main Results explicitly distinguish EGFβEGFR binding from absent direct MIFβEGF binding, and cellular labeled-EGF association is reduced by modified MIF. Preserve these separate pairs and roles. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26551075 EGF-receptor specificity for phosphotyrosine-primed substrat... | MODIFY | Summary: The MET-derived substrate interaction supports a scoped receptor-kinase class refinement. Reason: PMID26551075 tests a synthetic MET Tyr1234-region peptide as an EGFR substrate, with stronger phosphorylation of the primed peptide. Its sequence maps exactly to P08581 residues1229β1239, and official MET classification is receptor tyrosine kinase. The refinement identifies the parent protein class of this demonstrated substrate-fragment interaction; it does not claim that the fragment has receptor/kinase activity, that intact MET and EGFR form a complex in this experiment, or that a reference match proves the experimental natural isoform. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26751287 The LINK-A lncRNA activates normoxic HIF1Ξ± signalling in tri... | MODIFY | Summary: EGFR associates with GPNMB in a signaling assembly that recruits BRK. Reason: The original reports ligand-dependent EGFRβGPNMB association and interactions involving the GPNMB intracellular region. EGFR-dependent phosphorylation of GPNMB Tyr525 recruits BRK through BRKβs SH2 domain, placing GPNMB in a measured tethering role between signaling components. This supports scaffold protein binding rather than assigning kinase or other enzymatic activity to GPNMB. The SH2 interaction is BRKβs, not an asserted EGFR SH2 contact; the experiments also contain the separately described LINK-A scaffold. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27059931 Weak binding to E3 ubiquitin ligase c-Cbl increases EGFRvA p... | MODIFY | Summary: EGFR binds the E3 ligase CBL with a reported difference between wild-type receptor and EGFRvA. Reason: The authentic abstract reports weaker CBL association with EGFRvA than with wild-type EGFR, linked to altered receptor stability. The positive association and independently established CBL ligase class support the refinement. The operative full article was not recovered, so no detailed binding constants, construct sequence or isolated interface is asserted. Weak binding is not represented as absence, and CBL ubiquitin-transfer activity is not assigned to EGFR. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27569582 GOLM1 Modulates EGFR/RTK Cell-Surface Recycling to Drive Hep... | KEEP AS NON CORE | Summary: EGFR associates with GOLM1 in a receptor-recycling complex. Reason: The original identifies EGFR peptides in GOLM1-associated material and confirms the association by exogenous and endogenous co-immunoprecipitation in human liver-cancer cells. It maps an interaction to the short GOLM1 cytoplasmic region and links GOLM1 to EGFRβRAB11 complex formation. Retain this positive trafficking-complex association. The evidence is not enzyme activity of GOLM1, and a signaling-scaffold binding class is not inferred solely from a cargo-recycling assembly. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:2790960 Functional independence of the epidermal growth factor recep... | MODIFY | Summary: The EGFβEGFR interaction supports epidermal growth factor binding. Reason: The imported partner is EGF/P01133. The complete source abstract describes ligand-dependent receptor internalization and signaling by kinase-active receptor constructs; the independently authenticated ligandβectodomain structural abstract corroborates the specific ligand association. This supports EGF binding rather than an uninformative generic term. The original 1989 Methods were not recovered, so exact deletion coordinates, host cells and insert identity are not asserted from the abstract. Proposed replacements: epidermal growth factor binding |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | KEEP AS NON CORE | Summary: The source supports EGFRβSKAP2 association within the measured context. Reason: The original Results identify SKAP2 among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. SKAP2 is an adaptor associated with SRC signaling; it is not a kinase merely because of that association. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | MODIFY | Summary: EGFR associates with SRC in the reported interaction assay. Reason: The original Figure 6D/F and Results measure EGFRβSRC association by MaMTH in HEK293T reporter cells, with ROR2 and expression controls and modulation by PTPRA. This is a measured protein association, not binding inferred solely from downstream ERK activation. The independently captured official SRC record establishes the protein-kinase partner class; the refinement describes binding to that partner, not its catalytic activity as an EGFR function. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | MODIFY | Summary: EGFR binds the growth factor epiregulin. Reason: The original resolves the epiregulinβsEGFR501 structure and reports calorimetric binding. The ligand reagent is the human O14944 EGF-domain fragment D56βK116. The receptor construct is sEGFR501, expressed in Sf9 cells; the paper numbers the extracellular region from the mature chain, whereas the curated sequence interval is 25β525. The assayed human protein is not identified from the insect expression host. Growth factor binding describes this ligand without conflating it with EGF/P01133. No assay of every natural EGFR product is claimed. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29455656 The E3 ubiquitin ligase NEDD4 mediates cell migration signal... | MODIFY | Summary: EGFR associates with the E3 ubiquitin ligase NEDD4. Reason: The original reports EGF-dependent endogenous EGFRβNEDD4 co-immunoprecipitation in human lung-cancer cells and specifies anti-EGFR capture in the Methods. NEDD4βs independently verified E3 ligase activity supports the partner-class refinement. The association need not be a purified binary interaction, and it does not transfer ubiquitin-ligase activity to EGFR or imply identical behavior in every cell context. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:29844572 RANK-c attenuates aggressive properties of ER-negative breas... | KEEP AS NON CORE | Summary: EGFR association with the RANK-c product is retained with product-specific limits. Reason: The verified abstract reports association of the RANK-c variant with EGFR and effects on EGFR and NF-kappaB signaling. The imported Q9Y6Q6-2 product identifier is preserved. The ligand-receptor function of canonical full-length RANK is not automatically assigned to the distinct RANK-c product or used to force a receptor-binding refinement. The operative original and experimental insert sequence were not recovered, so the positive association is retained without claiming full-length receptor architecture or a purified interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30083275 The S100A4 Protein Signals through the ErbB4 Receptor to Pro... | MODIFY | Summary: The EGF positive control supports ligand-specific binding. Reason: The inspected Figure 1D EGF-LT/ErbB1 lane and label-transfer Methods support this pair independently of the paper's S100A4/ErbB4 survival mechanism. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30662352 COPI-Mediated Nuclear Translocation of EGFRvIII Promotes STA... | MODIFY | Summary: EGFRvIII associates with the SNARE protein syntaxin-6. Reason: The original reciprocal immunoprecipitations support EGFRvIIIβsyntaxin-6 association in human U251 cells, with starvation and nuclear-localization-sequence manipulations. Syntaxin-6βs established SNARE identity supports the more specific syntaxin-binding term. Human U251 experiments and separate rat C6 observations remain distinct. Paper and database residue-numbering conventions are not silently harmonized, and the engineered EGFRvIII result is not presented as evidence that all natural receptor products share this localization. Proposed replacements: syntaxin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | KEEP AS NON CORE | Summary: Retain the measured EGFRβSHC1 association within its source scope. Reason: Curated anti-tag coimmunoprecipitation records cite Figures 5F/G and S7D, retaining the EGFR P1019 mutant effects separately. The independently verified partner is a signaling adaptor. This source does not map a sufficiently specific partner-domain contact to replace the generic binding assertion; an SH2-containing protein is not automatically an isolated SH2 binding reagent. The project-specific policy retains supported generic binding as non-core. The complete publication abstract and detailed curator records were available, but the original full text and supplementary table were not recovered, so additional assay conditions are not asserted. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31862538 Neuropeptide bombesin receptor activation stimulates growth ... | MODIFY | Summary: EGFR associates with HER3 in the tested human lung-cancer cells. Reason: The original anti-HER3 immunoprecipitations recover EGFR after bombesin or neuregulin stimulation in human H441 and Calu-3 cells, with separate signaling and inhibitor experiments. HER3 is a receptor tyrosine kinase with impaired catalytic activity, which does not invalidate the partner class. This supports the binding refinement without claiming a purified binary interface, unrestricted HER3 catalysis, or activity of naturally truncated EGFR products. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped AIP association. Reason: The literal AIPβEGFR pair occurs at MYTH Interactome row 395 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. AIP is a receptor-associated co-chaperone/regulatory protein; its name alone does not establish a narrower ligand or protein-folding chaperone class. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33420426 AXL is a candidate receptor for SARS-CoV-2 that promotes inf... | KEEP AS NON CORE | Summary: The source reports EGFR association with SARS-CoV-2 spike without EGFR-mediated entry promotion. Reason: The original affinity-purification result is accompanied by tagged spikeβEGFR co-immunoprecipitation in HEK293T cells. Retain the positive association. In the same study EGFR overexpression did not promote viral entry, whereas AXL did; the purified binding experiment concerns AXL and must not be assigned to EGFR. The evidence therefore does not justify virus-receptor activity, an EGFR entry mechanism, or a purified EGFRβspike interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591612 A protein interaction landscape of breast cancer. | MODIFY | Summary: The breast-cell interaction map supports EGFR association with the enzyme FKBP5. Reason: The author-linked deposited network contains the exact EGFRβFKBP5 edge in MCF10A, derived from the studyβs tagged-bait affinity-purification/mass-spectrometry workflow. Its network attributes and cell context were recovered directly rather than inferred from the paper title. Independently verified FKBP5 peptidyl-prolyl isomerase activity supports enzyme binding, consistent with the separate LUMIER source. This does not transfer FKBP5 chemistry to EGFR or establish a purified interface; the deposition and reference sequence do not authenticate an exact experimental natural isoform. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | KEEP AS NON CORE | Summary: EGFR co-purifies with GRB2 in the published cancer-network dataset. Reason: The publication-linked NDEx deposit contains the exact EGFRβGRB2 edge and accession pair, with positive detection labels for SCC25, HET1A, CAL33. The main original describes triplicate inducible FLAG-bait affinity purification and mass spectrometry in two head-and-neck cancer lines and an immortalized comparator. These are physical co-complex measurements, not BioID-only proximity or a purified binary interface. The network also contains database-only edges, which are kept distinct; this selected edge has experimental detection labels. GRB2 is a noncatalytic signaling adaptor; the AP-MS experiment does not map an isolated SH2/SH3 interface. Retain the supported association as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the PIK3R2 association to phosphatidylinositol 3-kinase regulatory subunit binding. Reason: Dataset EV1A contains the literal PIK3R2βEGFR pair at EV1A row 7843 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This row is BioID-only and establishes proximity under the labeling conditions, not a purified binary contact. Independently read PMID:24658140 reports the same partner in a positive MaMTH association (source row 111); the narrower class uses that corroboration as well as this proximity record. The independently checked official PIK3R2 classification supports phosphatidylinositol 3-kinase regulatory subunit binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβAURKA association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official AURKA record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:37100772 Large-scale phage-based screening reveals extensive pan-vira... | MODIFY | Summary: An EGFR cargo motif binds the cargo-recognition domain of the AP-2 mu2 subunit. Reason: Authentic Supplementary Data 8 identifies the human EGFR 992β1007 peptide PTDSNFYRALMDEEDM binding human AP2M1 MHD, with a reported affinity of 2.4 Β± 0.1 micromolar. AP2M1 is the cargo-recognition subunit of AP-2, supporting a class-specific refinement for this mapped adaptor interface. The actual assay uses an isolated subunit domain and receptor peptide, not the complete AP-2 heterotetramer, full-length EGFR, or a cellular endocytosis measurement. The distinct IntAct Table S7/Figure 4b,c locators remain unchanged. Proposed replacements: AP-2 adaptor complex binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7518560 Hierarchy of binding sites for Grb2 and Shc on the epidermal... | MODIFY | Summary: The source directly assays the Shc SH2 interface. Reason: Recombinant Shc SH2 binding to human EGFR and receptor-site experiments support SH2 domain binding. Keep the paper fragment boundaries and the human-EGFR/murine-host distinction explicit; do not substitute the later PTB-dominance assay for this positive SH2 result. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7542744 The phosphotyrosine interaction domain of Shc binds an LXNPX... | MODIFY | Summary: The source explicitly supports binding to the Shc PTB domain. Reason: The complete abstract reports tests of the isolated PI/PTB recognition mechanism with phosphopeptides, protection assays and EGFR mutants. This supports PTB domain binding without relying on the presence of a domain elsewhere in SHC1. Full operative Methods and exact insert identity remain unverified. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7657591 Tyrosine phosphorylation of the c-cbl proto-oncogene protein... | MODIFY | Summary: The human CBL fragment interaction supports an E3-ligase partner class. Reason: The explicit GST-CBL 1β486 abstract result and two human far-western IntAct records support binding to the identified human CBL parent, independently classified as an E3 ubiquitin ligase. This does not claim autonomous ubiquitination by the assayed fragment or transfer that catalytic function to EGFR. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7685104 Substrate specificity of the protein tyrosine phosphatases. | MODIFY | Summary: Rat PTP1 recognizes an EGFR-derived phosphopeptide. Reason: The original rat PTP1 catalytic-fragment/EGFR-peptide assay supports protein phosphatase binding at substrate-contact resolution. Preserve rat P20417 and the peptide context; it is not an experiment on an intact endogenous human receptorβphosphatase complex. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7693694 Sequence specificity in recognition of the epidermal growth ... | MODIFY | Summary: The PLCG1 tandem-SH2 reagent directly resolves the interface. Reason: Original Methods/Results include a tandem-SH2 PLCG1 fusion and EGFR phosphotyrosine-site comparisons. SH2 domain binding captures this observed contact; no PLCG1 catalytic activity is assigned to EGFR, and complete construct species/sequence equivalence is not asserted. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7797556 Src phosphorylation of the epidermal growth factor receptor ... | MODIFY | Summary: The p85 association is resolved as Src-generated phosphotyrosine/SH2 docking. Reason: The complete abstract reports enhanced direct p85 binding to Src-phosphorylated EGFR and cellular association, explicitly linking the new sites to SH2 recognition; the official PIK3R1 record independently supports this receptor-docking mechanism. Refine the interface, while stating that full Methods and an isolated-domain construct were not recovered. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7993895 Identification of amino acids in the N-terminal SH2 domain o... | MODIFY | Summary: The N-terminal PLCG1 SH2 interface is explicitly assayed. Reason: The abstract identifies N-SH2 photo-crosslinking to EGFR phosphopeptides, competition and residue-mutation tests. This is domain-specific positive evidence. Keep modified-peptide and unresolved insert-species limits; it does not demonstrate every native full-length complex configuration. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:8034616 Tyrosines 1148 and 1173 of activated human epidermal growth ... | MODIFY | Summary: The original human Shc SH2 fragment supports this specific binding activity. Reason: The A172-derived Shc SH2 construct, paper residues 367β473, binds human EGFR in the original fragment and competition assays. These data remain valid even though other sources establish stronger PTB engagement in particular intact-cell contexts. Historical coordinates are not a current isoform assignment. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:8621392 Determinants of substrate recognition in the protein-tyrosin... | MODIFY | Summary: The rat PTP1 catalytic fragment contacts an EGFR substrate peptide. Reason: The source tests rat PTP1 residues 1β322 with a chemically modified EGFR phosphopeptide and competition/hydrolysis controls. Protein phosphatase binding describes the resolved parent class; preserve rat identity and avoid presenting the result as an intact human complex. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:8887653 The phosphotyrosine interaction domains of X11 and FE65 bind... | MODIFY | Summary: An explicit EGFRβGrb2 positive control supports binding to a scaffold-class partner. Reason: The APP-focused original contains an EGF-dependent GST-Grb2/EGFR control, corroborated by the literal IntAct record. GRB2 independently tethers multiple pathway members, including SOS, into signaling complexes, satisfying the current scaffold-protein definition. Whole GST-Grb2 was used here; do not relabel this particular assay as an isolated SH2 contact. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:8940013 The Grb2-mSos1 complex binds phosphopeptides with higher aff... | UNDECIDED | Summary: The positive mouse Grb2 assay leaves the imported human partner mapping unresolved. Reason: The original Methods specify murine Grb2 and murine mSos1 for the positive EGFR-phosphopeptide experiment, whereas this source row names human P62993. Current mouse and human references differ at residue 154, and neither reference comparison nor host identity establishes the experimental human insert. Retain the positive mouse result and the narrowly scoped dn/dc erratum; use UNDECIDED for this exact source-to-human-partner assertion, without alleging absent human binding or invalidating the biochemical result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | MODIFY | Summary: The PLCG1 tandem-SH2 capture reagent supports SH2 domain binding. Reason: The original uses a GST tandem-SH2 PLCG1 reagent to recover EGFR from A431 lysates. Preserve this explicitly assayed interface and distinguish it from whole-partner co-association measurements or autonomous phospholipase activity. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9050838 Development of "substrate-trapping" mutants to identify phys... | MODIFY | Summary: PTP1B substrate-trapping experiments support protein phosphatase binding. Reason: PTP1B D181A/C215A trapping and human-EGFR transfection experiments establish the enzymeβsubstrate contact with appropriate wild-type/EGFR controls. Keep the engineered trapping state and the separate COS versus 293 experiments explicit; this is not a claim that EGFR enables phosphatase catalysis. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9135143 Activation of HER4 by heparin-binding EGF-like growth factor... | MODIFY | Summary: The HER1 control explicitly supports EGF binding. Reason: The complete abstract includes positive EGF binding to HER1/EGFR, despite the main HER4 focus. Refine to epidermal growth factor binding while preserving the receptor-expression assay and unresolved exact ligand/insert details; do not transfer the distinct HER4 signaling conclusions. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9355745 Protein tyrosine phosphatase 1B interacts with and is tyrosi... | MODIFY | Summary: PTP1B trapping and purified-receptor experiments support its partner class. Reason: Selected original Methods/Results show specific PTP1B-C215S association with EGFR and A431-derived receptor experiments. Protein phosphatase binding is justified by the identified parent enzyme. Preserve trapping, COS1-host and experimental-sequence limits, without inferring a stable wild-type complex in every context. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9506989 Grb10 interacts differentially with the insulin receptor, in... | MODIFY | Summary: The human GRB10 SH2 fragment mediates the assayed EGFR interaction. Reason: The original tests human GRB10 SH2 residues 435β536 in paper numbering, with loss of EGFR binding after R462K; the BPS fragment does not supply the EGFR interface. Refine to SH2 domain binding and retain construct-specific coordinates rather than assigning an unverified current isoform. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9544989 Shc phosphotyrosine-binding domain dominantly interacts with... | MODIFY | Summary: The p52 Shc PTB domain is the dominant tested EGFR interface in this context. Reason: Human p52 Shc PTB/SH2 mutants and human EGFR variants in CHO cells resolve a predominant PTB interaction. Refine this source to PTB domain binding while retaining the residual context-dependent SH2 contribution and avoiding an all-isoform or universal exclusion claim. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:16777603 An allosteric mechanism for activation of the kinase domain ... | ACCEPT | Summary: EGFR kinase-domain self-association contributes to allosteric receptor activation. Reason: Retain the curated positive self-binding annotation. PMID:16777603 combines human EGFR kinase-domain structural and biochemical evidence with interface-mutant tests in full-length receptor. The purified domain is residues 672β998 in the paper's mature-protein numbering and was produced in Sf9 cells; receptor signaling was tested in NIH3T3 cells. Artificial His-tag recruitment to lipid vesicles increases local concentration. The current IntAct record identifies PDB 2GS7, which the original describes as the inactive V924R mutant, so that individual structure must not be represented as a native wild-type active dimer. The paper's combined interface and functional evidence supports gene-level self-association without asserting every product or mutant behaves identically. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | ACCEPT | Summary: The EGFR extracellular/transmembrane constructs undergo ligand-dependent homooligomerization. Reason: The original Results and Figure4 report EGF-induced complementation between EGFR1β679 fusion constructs in C2C12 cells. This supports the existing self-association annotation at the construct level. It does not measure full-length receptor kinase activity or establish a stable native oligomer stoichiometry. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:18042729 Epidermal growth factor receptor juxtamembrane region regula... | ACCEPT | Summary: Differently tagged wild-type EGFR intracellular domains coassociate in cells. Reason: PMID:18042729 Fig. 4 and the operative Methods directly compare wild-type Myc- and FLAG-tagged EGFR intracellular domains with juxtamembrane deletions and T654D. The authors subtract tag cross-reaction and assess reciprocal precipitation; wild-type association is the positive comparison. These are engineered intracellular domains (paper residues 645β1186) in COS-7 cells, with separate full-length activation tests in NIH3T3 cells, not an endogenous human-cell dimer isolation. The original construct source is identified but its complete sequence and natural isoform were not independently mapped. This physical association supports the core self-binding annotation; the loss or reduction in particular mutants does not negate wild-type binding. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:19563760 Mechanism for activation of the EGF receptor catalytic domai... | ACCEPT | Summary: Human EGFR kinase constructs self-associate in the activation study. Reason: The independent source assessment documents kinase/juxtamembrane self-association and a separate human full-length FLAG-EGFR experiment in COS7 cells. HER4 structural comparisons are distinguished from direct EGFR experiments. A linked erratum is bibliographically verified but its scope is unresolved; no precise kinetic values or mutation-role assignments are adopted here. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:19650109 Flow cytometric in situ proximity ligation analyses of prote... | ACCEPT | Summary: EGFR self-association is supported by complementary receptor experiments. Reason: The source reports a homomeric EGFR PLA signal, with limited change after EGF under its tested conditions. Independent complementation experiments support EGFR self-association. The PLA measurement is treated as proximity evidence within this combined account, not as a purified dimer-interface assay or proof of fixed native stoichiometry. |
| GO:0042802 identical protein binding | IPI PMID:20007378 Structural analysis of the catalytically inactive kinase dom... | ACCEPT | Summary: EGFR kinase-domain self-association is supported within a study centered on HER3. Reason: The title of PMID:20007378 does not indicate an EGFR misattribution. Selected original Results and Fig. 3 explicitly assay EGFR kinase-domain constructs (paper residues 672β998) on lipid vesicles alongside HER3, including the EGFR positive comparison and asymmetric-interface perturbations. The Methods describe concentration-dependent, His-tag-mediated vesicle recruitment and a coupled kinase assay. The new crystal structure and the proposed HER3/HER4 oligomeric lattice belong to those paralogs; they are not new structures of EGFR homooligomers. Retain the curator's EGFR self-binding assertion, supported by the EGFR assays and independent human EGFR structural evidence in PMID:16777603, without transferring HER3-specific lattice behavior or claiming an unmodified full-length human receptor was assayed here. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | ACCEPT | Summary: The split-ubiquitin assay supports EGFR self-association. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The exact curated self-pair is positive and contains EGFR on both sides. This supports homotypic receptor association under the tested membrane-assay conditions; it does not establish ligand-driven phosphorylation, single-molecule stoichiometry or equivalence of natural truncated products. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:20359299 A proximity ligation assay using transiently transfected, ep... | ACCEPT | Summary: Tagged human EGFR molecules produce a ligand-responsive self-association PLA signal. Reason: The authentic abstract of PMID:20359299 directly identifies coexpressed FLAG- and MYC-tagged human EGFR and biological controls for ligand-dependent dimer detection. The saved IntAct record specifies CHO-K1 host cells and Figures 3β5; it preserves separate tag and interaction-reducing mutation features. Retain the positive curated assertion because it matches established EGFR self-association. PLA reports proximity consistent with association and the abstract reports control validation, but the operative full Methods were inaccessible in this audit. Do not claim a purified binary interface, a particular dissociation constant, or independently verified mutant mapping from this record alone. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | UNDECIDED | Summary: The source-specific EGFR self-association assay remains unresolved. Reason: The inspected main text and unrecovered supplement do not resolve this imported positive. This is an access limitation, not evidence against EGFR self-association. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:21480528 Comparative analysis of fluorescence resonance energy transf... | ACCEPT | Summary: Curated EGFR self-association is supported by FRET and PLA records in A431 cells. Reason: The literal PMID:21480528 IntAct records independently identify EGFRβEGFR FRET and PLA experiments in human A431 cells at supplemental Figure S1A; the FRET record includes EGF stimulation. The authentic abstract cautions that PLA saturates and is semiquantitative, including for intramolecular signals. Retain the curator-supported, biologically established self-binding term, while distinguishing these two assay types from a purified binary interface or exact stoichiometry. The complete Methods and supplemental figure were not recovered, so their antibody geometry and control results were not independently inspected. No misattribution or false interaction is inferred from this access limitation. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:21482778 Quantification of receptor tyrosine kinase transactivation t... | ACCEPT | Summary: Fluorescence lifetime and brightness measurements support EGFR association in cells. Reason: PMID:21482778 selected original Results and Fig. 1 describe EGF-responsive EGFR-GFP/EGFR-mCherry FLIM-FRET and calibrated SpIDA dimer-density measurements in CHO-K1 cells. The monomeric-GFP calibration, receptor lifetime control and Rab5 S34N comparison address brightness and large-cluster effects. These are cell-based tagged-receptor association measurements, not purified direct binding or proof that every fluorescent cluster is a dimer. The host is hamster; the complete insert sequence and natural product were not independently verified. Retain the positive self-binding annotation. The paper's endogenous-neuron experiment concerns TrkB and must not be relabeled as endogenous neuronal EGFR self-binding. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:22232519 In situ analysis of mutant EGFRs prevalent in glioblastoma m... | ACCEPT | Summary: Wild-type EGFR self-association is distinguished from cancer-associated mutant pairings. Reason: PMID:22232519 includes a wild-type EGFRβEGFR positive pairing as well as vIII and truncated mutant pairings. The saved IntAct CHO-K1 record specifies differently tagged partners and explicitly records the EGF-responsive wild-type pairing; the separate human glioblastoma record concerns wild-typeβvIII association. The authentic abstract and selected publisher text support this distinction. Retain wild-type self-binding as a core receptor property, without treating mutant heteropairs as identical natural products or claiming that all mutant combinations require ligand. Complete operative Methods and figure pixels were not recovered, so the exact constructs and per-condition measurements are not independently revalidated here. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:22579287 Oncogenic mutations counteract intrinsic disorder in the EGF... | ACCEPT | Summary: EGFR kinase self-association is modulated by an oncogenic substitution. Reason: The authentic PMID:22579287 abstract separates molecular-dynamics predictions from biophysical and kinase experiments supporting increased dimerization by L834R, also designated L858R. The saved IntAct entries identify light scattering and native-gel comigration at Fig. 4A/B; their literal feature coordinates are retained separately and are not equated to the abstract's mutation number. Retain the curated positive EGFR self-binding annotation, which is independently established for human EGFR, while limiting this source to the reported kinase-domain and oncogenic-mutant comparison. The full operative body was inaccessible; this audit does not infer an exact construct sequence, all-isoform behavior, or ligand dependence of every mutant. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:23273428 Insights into the aberrant activity of mutant EGFR kinase do... | UNDECIDED | Summary: The cited mutant-kinase study does not yet provide a verified source-specific EGFR self-binding assay here. Reason: EGFR self-association is biologically well supported, but the recovered abstract and inspected 4I21 deposition establish mutant kinase conformations and an EGFRβMIG6 heteromer, not the particular identical-protein interaction represented by this source row. The two receptor copies in the crystal are not automatically interpreted as a physiological homodimer: the deposited biological assemblies are separate receptorβMIG6 heterodimers. The full operative article and other source-specific self-association evidence remain unrecovered, so the imported positive assertion is retained as unresolved rather than rejected. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:23374349 Conformational coupling across the plasma membrane in activa... | ACCEPT | Summary: EGFR self-association couples membrane and intracellular receptor regions. Reason: The original Results use pulsed-interleaved fluorescence cross-correlation in live cells to distinguish oligomerization from random collisions and spectral cross-talk; EGF increases full-length EGFR association in the measured surface-density range. NMR of the reported TM-JM fragment, residues 618β673 in the paper's numbering, provides intermolecular contacts in lipid bicelles. These experiments support self-binding while separating engineered fragments, membrane conditions and full-length receptor behavior. Main Methods were read; the extended supplement and exact natural-product insert sequence were not authenticated. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | ACCEPT | Summary: EGFR self-association is supported independently of the proximity-ligation signal. Reason: The source reports EGFR proximity ligation in cellular and tumor contexts, which alone does not establish a molecular interface. The independently read live-cell cross-correlation and transmembrane/juxtamembrane NMR study supports EGFR self-association. The combined evidence supports identical protein binding without assuming every observed proximity pair is a constitutive dimer or that tail autophosphorylation itself causes allosteric activation. |
| GO:0042802 identical protein binding | IPI PMID:23636329 EGFR modulates microRNA maturation in response to hypoxia th... | UNDECIDED | Summary: The source-specific EGFR self-binding evidence remains unresolved. Reason: The accessible original primarily establishes heterotypic EGFRβAGO2 association through co-immunoprecipitation, pull-down and split-YFP experiments. Those positive results cannot alone verify this separate identical-protein-binding assertion. The relevant supplemental material was not recovered despite bounded access attempts. This is uncertainty about the source-specific assay, not a claim that EGFR cannot self-associate, and no negative conclusion is drawn from the paper main-text emphasis. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:24135280 EGFR phosphorylates tumor-derived EGFRvIII driving STAT3/5 a... | UNDECIDED | Summary: This citation does not yet resolve a physical EGFRβEGFRvIII self-association. Reason: The literal source-linked records concern colocalization. The recovered original also reports unsuccessful co-immunoprecipitation of wild-type EGFR with EGFRvIII under the tested conditions, while their nuclear associations with STAT3 are separately positive. Colocalization alone does not verify this self-binding assertion, and a negative co-immunoprecipitation under one condition does not establish universal nonbinding. Preserve the source record with source-specific uncertainty rather than importing dimerization evidence from other papers. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | ACCEPT | Summary: EGFR self-association is ligand- and construct-dependent. Reason: The original combines extracellular-domain structures and solution SAXS with FRET of human EGFR extracellular/transmembrane constructs in CHO-derived membrane vesicles. Epiregulin and epigen induce weaker, density-dependent association than EGF, while the epigen-bound crystallized fragment is monomeric. Full-length receptor tracking provides a separate mobility readout, whose interpretation also includes signaling-complex assembly. These results support self-association without treating FRET proximity alone as a mapped interface, claiming universal stable dimers or assigning the fragments to a natural short product. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | ACCEPT | Summary: Retain the source-scoped EGFR association. Reason: The literal EGFRβEGFR pair occurs at MYTH Interactome row 403 (published MYTH/IID integrated network); mtKRAS_Hi interactions row 594 (AP-MS mtKRAS_Hi interactions); mtKRAS_Lo interactions row 500 (AP-MS mtKRAS_Lo interactions). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The separately listed AP-MS rows recover the complex in the indicated human colorectal-cell KRAS contexts; co-purification does not map a binary interface. The integrated network explicitly records EGFR self-association, consistent with its receptor dimer mechanism. Recovery of the bait itself in AP-MS is not, on its own, independent proof of a homodimer, and no exact stoichiometry or allosteric state is inferred from these network rows. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | ACCEPT | Summary: The tested receptor pair supports EGFR self-association. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. Both pair members are EGFR. Homotypic receptor association is consistent with the core receptor mechanism, while this assay does not resolve ligand dependence, catalytic activation or native oligomer stoichiometry. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:38572507 DRD1 suppresses cell proliferation and reduces EGFR activati... | ACCEPT | Summary: EGFRβEGFR proximity in human lung cancer cells is a supporting self-association readout. Reason: PMID:38572507 Methods and Fig. 2F/G use rabbit and mouse anti-EGFR antibodies for PLA in human H1299 cells, explicitly treating EGFRβEGFR as an assay positive control. The Results describe a reduced signal after DRD1 overexpression together with reduced EGFR expression and activation. Retain the biologically established curator-supported self-binding assertion, but this experiment alone does not distinguish intermolecular binding from all same-target antibody-proximity contributions, determine dimer stoichiometry, or isolate a change in binding affinity from receptor abundance. The DRD1βEGFR PLA and downstream tumor phenotypes are separate claims and are not required for this annotation. Supporting Evidence: |
| GO:0007165 signal transduction | TAS Reactome:R-HSA-212718 | MODIFY | Summary: Refine to epidermal growth factor receptor signaling pathway in the explicit EGFR catalytic context. Reason: In R-HSA-212718 (EGFR interacts with phospholipase C-gamma), the captured typed path 212718 --hasEvent--> 212710; 212710 --catalystActivity--> 212705; 212705 --activeUnit--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The pathway contains the explicit EGFR active-unit step phosphorylating PLCG1. The generic signal-transduction term is therefore refined to the existing EGF receptor signaling pathway, without assigning phospholipase activity to EGFR. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor signaling pathway Supporting Evidence: Reactome:R-HSA-212718 |
| GO:0007173 epidermal growth factor receptor signaling pathway | TAS Reactome:R-HSA-177929 | ACCEPT | Summary: Retain epidermal growth factor receptor signaling pathway with the exact EGFR entity and event scope. Reason: In R-HSA-177929 (Signaling by EGFR), the captured typed path 177929 --hasEvent--> 177934; 177934 --catalystActivity--> 9624430; 9624430 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. This defining receptor pathway contains explicit EGFR catalytic steps, rather than merely consuming EGFR as a substrate. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177929 |
| GO:0042059 negative regulation of epidermal growth factor receptor signaling pathway | TAS Reactome:R-HSA-182971 | ACCEPT | Summary: Retain negative regulation of epidermal growth factor receptor signaling pathway with the exact EGFR entity and event scope. Reason: In R-HSA-182971 (EGFR downregulation), the captured typed path 182971 --hasEvent--> 182969; 182969 --catalystActivity--> 183047; 183047 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The downregulation pathway includes EGFR phosphorylation of CBL (event 182969; catalyst 183047; EGFR activeUnit 179837). That catalytic contribution to feedback supports participation beyond the receptor simply undergoing ubiquitination or degradation. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-182971 |
| GO:0000902 cell morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse cell-morphogenesis context is supported at the curated donor level. Reason: The current Q01279 record is IGI to PMID:17686994. Its abstract foregrounds SYT-SSX2 and EphB2, so the available evidence does not reconstruct the EGFR-specific genetic experiment from the abstract. This is not evidence of a wrong-gene annotation. Retain the broad, non-core morphogenetic context with the imported upstream-or-within qualifier; do not claim a directly assayed human morphogenetic mechanism. Supporting Evidence: |
| GO:0001892 embryonic placenta development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Placental development is a context-dependent consequence of EGFR signaling. Reason: The current mouse IMP donor cites PMID:7618084. The abstract explicitly reports strain-dependent placental death of Egfr-null embryos, rather than a universal phenotype in every background. Preserve that developmental context and the human orthology-transfer boundary; necessity is not used to invent a new direct placental activity. Supporting Evidence: |
| GO:0001942 hair follicle development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Hair-follicle development remains a supported developmental context. Reason: Current mouse IMP/IGI records cite PMID:7618084 and PMID:9030684. The available abstracts describe Egfr-null tissue abnormalities and a sensitized Sos1/Egfr genetic context; they do not resolve every follicular stage. Retain the existing broad tissue outcome without manufacturing a more specific human follicle mechanism. |
| GO:0005006 epidermal growth factor receptor activity | IEA GO_REF:0000120 | ACCEPT | Summary: EGF receptor activity is supported by direct experimental donor records and conserved receptor biology. Reason: The complete mouse capture contains multiple experimental GO:0005006 records, including the ligand-binding/receptor-phosphorylation context of PMID:7678348 and kinase-dependent intestinal signaling in PMID:18701712. Propagated ISO/IEA records are kept separately from those experimental records. These donor records corroborate the mouse transfer arm, not every ARBA condition or every EGFR isoform. |
| GO:0006511 ubiquitin-dependent protein catabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR contributes to the machinery controlling its ubiquitin-dependent downregulation. Reason: The receptor contribution extends beyond being a degradation substrate. PMID:11823423 shows that the receptor provides phosphorylated CBL/GRB2 docking sites and kinase-dependent recruitment supporting ubiquitination and downregulation; CBL supplies the ubiquitin-ligase activity and lysosomal machinery performs degradation. This supports a non-core upstream contribution, not EGFR protease activity. No exact current Q01279 GO:0006511 record was recovered, so this is independent mechanistic corroboration rather than a reconstructed historical Ensembl donor. The assayed receptor constructs were expressed in several cell hosts; their species and exact current product sequence are not established by the inspected Methods. Supporting Evidence: |
| GO:0007165 signal transduction | IEA GO_REF:0000107 | MODIFY | Summary: The receptor-specific signaling pathway is more informative than generic signal transduction. Reason: The current generic mouse IDA cites PMID:11940581; its abstract describes rat vascular smooth-muscle and CHO experiments, so mouse-specific construct provenance is not independently recovered here. Independent current mouse receptor-pathway experiments establish the narrower EGFR signaling claim. Refine to the already represented GO:0007173 as biological precision, without changing the imported donor identities or alleging a wrong-species curation error. Proposed replacements: epidermal growth factor receptor signaling pathway |
| GO:0007173 epidermal growth factor receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: EGFR is an initiating receptor of its own signaling pathway. Reason: Multiple current mouse experimental GO:0007173 records support the receptor pathway, including ligand-induced receptor activation and kinase-dependent signaling. Its own initiation of the pathway is direct participation; this does not automatically prove a distinct positive-regulation process for row208. |
| GO:0007435 salivary gland morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Salivary-gland morphogenesis is a supported developmental context. Reason: The current mouse IMP cites PMID:10521784, whose abstract reports decreased branching in Egfr-null submandibular glands. Retain the tissue-specific signaling contribution without promoting gland morphogenesis to a distinct molecular activity or claiming a direct human embryonic assay. Supporting Evidence: |
| GO:0008283 cell population proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR signaling acts upstream of cell proliferation. Reason: No exact current Q01279 GO:0008283 record was returned, so its historical donor cannot be reconstructed from the present snapshot. Current related experimental positive-proliferation records and the ligand-dependent mitogenic comparisons in PMID:11823423 corroborate the broad biological claim. Preserve the imported acts_upstream_of qualifier rather than describing EGFR as the cell-cycle machinery itself. |
| GO:0008284 positive regulation of cell population proliferation | IEA GO_REF:0000107 | ACCEPT | Summary: Positive regulation of cell population proliferation is a principal EGFR signaling output. Reason: Current Q01279 experimental records include PMID:18656477, whose mouse betacellulin-induced crypt proliferation is abolished by a dominant-negative EGFR. The other current donors remain literal evidence records; their details are not inferred from titles. This ortholog evidence supports the same mitogenic role as the human EGFR depletion evidence in PMID:27057632. Accept that gene-level role while preserving the mouse intestinal context and without asserting a universal proliferative response across tissues. |
| GO:0008544 epidermis development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Epidermal development is a supported tissue context. Reason: Mouse IMP to PMID:7618084 supports skin abnormalities after Egfr loss, with genetic-background-dependent survival. Retain the broad developmental assertion and avoid an unverified stage-specific human mechanism. Supporting Evidence: |
| GO:0009986 cell surface | IEA GO_REF:0000120 | ACCEPT | Summary: The cell surface is a supported receptor location. Reason: The exact current mouse IDA cites PMID:23918928. Its abstract foregrounds proprotein convertases and does not expose the EGFR-specific control, so that experiment is not reconstructed here and is not dismissed as misattributed. Independent receptor surface-ligand/internalization measurements in PMID:11823423 corroborate the location. No membrane topology beyond the source claim is manufactured. |
| GO:0010467 gene expression | IEA GO_REF:0000107 | UNDECIDED | Summary: The source-specific gene-expression mechanism remains unresolved. Reason: The current mouse IMP cites PMID:28790147. The accessible abstract reports lower ABCG2 and increased ABCB1 protein levels after hepatocyte Egfr deletion, but does not establish whether production, turnover, or another step explains the abundance change. The full original was not recovered after a publisher access failure. Preserve the positive donor assertion, but do not turn steady-state protein abundance into a direct transcription or gene-expression mechanism. This access uncertainty is narrower than the measured transport phenotype at row207. Supporting Evidence: |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Basolateral localization is supported in polarized epithelia. Reason: Current mouse IDA to PMID:7723235 describes basolateral EGFR in control proximal and collecting tubules, with altered apical/lateral distribution in cystic collecting tubules. The polarized location is valid but contextual. This is consistent with the independent PAINT advice on basolateral localization and does not negate the principal plasma-membrane pool. Supporting Evidence: |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR actively recruits the machinery for its own ubiquitination. Reason: CBL is the ubiquitin ligase; EGFR is not assigned ubiquitin-transferase activity. Nevertheless PMID:11823423 demonstrates an active receptor contribution through phosphorylated CBL/GRB2 docking and receptor-kinase-dependent signaling, so the receptor is not merely an inert substrate. Retain the existing upstream-or-within process context as non-core with this corrected reason. No exact current Q01279 GO:0016567 record was recovered; the mechanistic support is independent of, rather than a claimed reconstruction of, the historical transfer. Construct species is not inferred from the 32D/CHO/HEK host cells. Supporting Evidence: |
| GO:0021795 cerebral cortex cell migration | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cortical-cell migration is a curated developmental context. Reason: The current mouse IMP to PMID:7618084 supports the inherited developmental assertion at curator level. The abstract reports brain abnormalities but does not independently resolve cortical-migration cell types or stages. Retain the contextual transfer without asserting a directly assayed human migration mechanism or rejecting a curator from the abstract alone. Supporting Evidence: |
| GO:0030139 endocytic vesicle | IEA GO_REF:0000120 | ACCEPT | Summary: Endocytic vesicles are a supported receptor-trafficking location. Reason: The current mouse IDA cites PMID:10534613; its ectodysplasin-focused abstract does not reveal the EGFR-specific control, which remains a source-access limit rather than evidence of a wrong-gene annotation. Independent PMID:11823423 Results and Figure2 caption document ligand-induced EGFR relocation into endocytic vesicles. Keep the location while preserving both provenance layers. |
| GO:0038134 ERBB2-EGFR signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR participates in signaling with ERBB2. Reason: Current mouse experimental records include PMID:18701712 and PMID:21897861. Their abstracts describe receptor phosphorylation, loss/inhibition/rescue signaling effects and ERBB1/ERBB2-dependent responses. These support pathway participation, without asserting identical ligand preferences for all ERBB dimers or inferring the species of every introduced construct from the host. |
| GO:0042059 negative regulation of epidermal growth factor receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: Receptor docking and kinase-dependent recruitment contribute to negative feedback. Reason: PMID:11823423 directly tests EGFR docking-site/kinase mutants and CBL/GRB2-dependent ubiquitination, internalization and signaling suppression; this is more than EGFR simply being degraded. The separate current donor PMID:23457600 measures berberine-induced CBL activation and EGFR downregulation, with the CBL activation mechanism unresolved and reduced EGFR-Y1045 phosphorylation in that condition. That second paper alone does not establish that EGFR activates its own negative regulator. Retain the integrated feedback assertion with the first source and explicit construct/host limits. |
| GO:0042127 regulation of cell population proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Proliferation regulation is context dependent. Reason: The current mouse IGI cites PMID:11818567. Its abstract distinguishes reduced establishment of intestinal adenomas from the largely EGFR-independent size/expansion of established polyps, while a separate human cancer-cell xenograft experiment responds to inhibition. Retain the contextual regulatory claim rather than universal proliferation dependence. Supporting Evidence: |
| GO:0042908 xenobiotic transport | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR acts upstream of xenobiotic transport in a mouse hepatocyte context. Reason: Two current MGI IMP records cite PMID:28790147; one retains occurs_in EMAPA:32874 and has_input CHEBI:114785. The abstract reports hepatocyte Egfr deletion changing radiolabeled erlotinib biliary/urinary handling and transporter abundance. This is positive evidence of contextual upstream regulation, not proof that EGFR is a transporter. The inherited not-a-transporter rationale is therefore insufficient for over-annotation. Keep the existing acts_upstream_of_or_within assertion non-core; no directly assayed human transport mechanism, autonomous transport activity or unverified full-text details are claimed. Supporting Evidence: |
| GO:0045742 positive regulation of epidermal growth factor receptor signaling pathway | IEA GO_REF:0000107 | UNDECIDED | Summary: A distinct positive-regulatory EGFR-pathway role is not resolved by this transfer. Reason: The complete current Q01279 snapshot contains no exact GO:0045742 record, so the original experimental donor behind this historical electronic assertion is not reconstructed. Receptor initiation establishes participation in GO:0007173, but does not by itself identify a separate positive-regulatory mechanism. Retain uncertainty rather than inventing such a mechanism or treating absence from current GOA as curator rejection. No loss of the established receptor pathway is implied. |
| GO:0048146 positive regulation of fibroblast proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fibroblast proliferation is a supported contextual output. Reason: The current mouse IMP cites PMID:20208556. Its abstract reports presenilin/Fbw7-dependent control of EGFR stability and enhanced signaling/proliferation in the relevant fibroblast context. Preserve the existing process assertion without generalizing the sensitized setting to every fibroblast or human tissue. Supporting Evidence: |
| GO:0048408 epidermal growth factor binding | IEA GO_REF:0000107 | ACCEPT | Summary: EGF binding is supported by direct mouse ligand-binding evidence. Reason: The current mouse IDA cites PMID:7678348. Its abstract explicitly describes radiolabeled EGF binding, receptor immunostaining and EGF-inducible tyrosine phosphorylation in mouse blastocysts. This supplies experimental grounding for the conserved ligand-binding function. The additional IBA/ISO records are not counted as independent experiments. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Perinuclear localization remains a curated contextual pool. Reason: The current mouse IDA cites PMID:20208556. The abstract does not locate the imaging assay, so the assessment relies on the literal curated location record rather than inventing its compartment or trafficking route. Keep the non-core pool with this access boundary; do not reduce a positive source annotation to unsupported speculation. Supporting Evidence: |
| GO:0048546 digestive tract morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Digestive-tract morphogenesis is a supported developmental context. Reason: Current mouse IMP to PMID:7618084 supports gastrointestinal abnormalities in an Egfr-null genetic background. The abstract does not resolve every anatomical substage, and the human row remains an orthology transfer. Retain the broad contextual assertion without a new direct morphogenetic activity. Supporting Evidence: |
| GO:0050673 epithelial cell proliferation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR acts upstream of epithelial proliferation. Reason: The exact historical GO:0050673 donor is absent from the current snapshot, but related current mouse positive-regulation records and PMID:18656477 corroborate epithelial proliferation as a signaling outcome. Preserve the source acts_upstream_of qualifier and avoid claiming that the receptor itself executes the cell cycle. |
| GO:0050679 positive regulation of epithelial cell proliferation | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Positive epithelial-proliferation regulation is a supported tissue outcome. Reason: The current mouse IMP cites PMID:7618084, and the independent mouse betacellulin/EGFR experiment in PMID:18656477 supplies corroborating proliferation evidence. This is a contextual consequence of receptor signaling rather than a distinct catalytic core. The ARBA arm is preserved and is not reclassified from this donor-only consultation. |
| GO:0060571 morphogenesis of an epithelial fold | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Epithelial-fold morphogenesis remains a curated developmental context. Reason: Current mouse IMP to PMID:7618084 supports the source assertion at curator level. The abstract does not resolve the particular fold or stage, so no more specific mechanism or human experimental claim is added. Retain the existing contextual transfer rather than second-guessing a full-text curation from its abstract. Supporting Evidence: |
| GO:0061029 eyelid development in camera-type eye | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Eyelid development is supported in a sensitized mouse genetic context. Reason: The current mouse IGI cites PMID:9030684. The abstract reports enhanced eye defects when Sos1 dosage is reduced in the hypomorphic Egfr-wa2 background. Retain the developmental context without claiming a direct human eyelid assay or universal effect of every EGFR perturbation. Supporting Evidence: |
| GO:0070086 ubiquitin-dependent endocytosis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: EGFR contributes docking and kinase-dependent recruitment to ubiquitin-linked endocytosis. Reason: PMID:11823423 compares wild-type, Y1045F and kinase-defective receptor constructs, with CBL/GRB2 recruitment, ubiquitination and internalization assays. This supports an active upstream receptor contribution rather than retention merely because EGFR is endocytosed. The ubiquitin-conjugating and membrane-remodeling machinery remains distinct from receptor activity. No exact current Q01279 GO:0070086 record was recovered; independent mechanistic support does not reconstruct the historical donor or establish a current isoform-specific assay. Supporting Evidence: |
| GO:0071230 cellular response to amino acid stimulus | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: The cited amino-acid response measures EGFR translation as an output. Reason: The current mouse IDA points to PMID:22711986. The inspected original Results, Methods and Figure1 caption concern NMDA-triggered calpain/CPEB3 control of EGFR translation in rodent neurons, with a rat EGFR 3-prime-UTR explicitly used in part of the analysis. EGFR abundance is the response readout; an active EGFR step in that response is not established in the inspected experiment. The inherited amino-acid-availability signaling explanation is inaccurate. Mark this human electronic involved_in transfer as over-annotated while preserving the positive rodent translation result; do not claim that EGFR cannot mediate other neuronal responses. Supporting Evidence: |
| GO:0071363 cellular response to growth factor stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cellular growth-factor responses are supported contextual signaling outcomes. Reason: Current mouse IDA cites PMID:8702723. The abstract compares ligand-dependent receptor phosphorylation and survival/proliferation in engineered mouse Ba/F3 cells expressing ERBB receptors singly or in pairs. The host identity does not establish every receptor construct species. Retain the broad response context without treating all ERBB ligand/dimer combinations as equivalent. Supporting Evidence: |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | TAS Reactome:R-HSA-177930 | MODIFY | Summary: Refine to epidermal growth factor receptor activity in the explicit EGFR catalytic context. Reason: In R-HSA-177930 (GAB1 phosphorylation by EGFR kinase), the captured typed path 177930 --catalystActivity--> 180302; 180302 --activeUnit--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The catalyst activity matches the imported kinase term and explicitly identifies EGFR as activeUnit. In this ligand-activated membrane-receptor context, the existing EGFR receptor activity is the more informative integrated activity; the catalytic reaction is not inferred from membership in another enzyme's complex. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: Reactome:R-HSA-177930 |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | TAS Reactome:R-HSA-177933 | MODIFY | Summary: Refine to epidermal growth factor receptor activity in the explicit EGFR catalytic context. Reason: In R-HSA-177933 (SHC1 phosphorylation by phosphorylated EGFR), the captured typed path 177933 --catalystActivity--> 9624433; 9624433 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The catalyst activity matches the imported kinase term and explicitly identifies EGFR as activeUnit. In this ligand-activated membrane-receptor context, the existing EGFR receptor activity is the more informative integrated activity; the catalytic reaction is not inferred from membership in another enzyme's complex. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: Reactome:R-HSA-177933 |
| GO:0005515 protein binding | IPI PMID:39073202 SNX32 Regulates Sorting and Trafficking of Activated EGFR to... | KEEP AS NON CORE | Summary: The source reports EGFR binding to the endosomal sorting protein SNX32. Reason: The verified primary abstract explicitly reports direct EGFR binding by SNX32 and recruitment of SNX5 during endosomal sorting. This supports the imported positive protein-binding assertion. The operative full article and target-resolved construct details were not recovered, so no detailed purified assay, binding-domain assignment or natural-product equivalence is asserted. A role in cargo sorting alone does not establish that SNX32 is an enzyme or justify an unsupported more specific binding class. Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:12828935 Activation of epidermal growth factor receptor signals induc... | ACCEPT | Summary: EGFR activity is implicated in the optic-nerve-head astrocyte response. Reason: The complete source abstract reports activation of EGFR in human optic-nerve-head astrocytes and connects it to NOS2 induction in vitro and in glaucomatous tissue. This supports the established receptor function at the source's stated scope. The unavailable original Methods do not establish a particular natural isoform or purified enzyme kinetics. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:20462955 A G{alpha}i-GIV molecular complex binds epidermal growth fac... | ACCEPT | Summary: EGF-bound EGFR is directly tracked at the plasma membrane. Reason: The study follows endogenous EGFR in human HeLa cells using HRP-EGF, surface/permeabilized staining and endosomal imaging. GIV perturbations alter receptor retention and internalization. This provides source-specific evidence for the plasma-membrane receptor pool, rather than inferring location solely from a transmembrane segment; it does not make every later intracellular pool equivalent. Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | ACCEPT | Summary: Ligand-activated EGFR drives signaling in human esophageal keratinocytes. Reason: The original Methods use primary human EPC1/EPC2 cells expressing the entire human EGFR coding sequence, with sequence checking of the expression construct. EGF-dependent receptor phosphorylation and downstream Akt/STAT1 responses, together with EGFR inhibition, support the receptor signaling pathway. The human-cell experiments are distinct from the transgenic mouse tissue expressing human EGFR. Supporting Evidence: |
| GO:0005768 endosome | IDA PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | ACCEPT | Summary: EGFR-containing internal vesicles are observed in the DGK-theta trafficking study. Reason: The complete abstract reports that DGK-theta first reaches the plasma membrane and then internalizes into EGFR-containing vesicles after EGF stimulation in A431 cells. This positive trafficking account is consistent with the curated endosome annotation and the independently established receptor compartment. The inaccessible original Methods do not justify a particular endosomal marker or an early-versus-late subtype claim. Supporting Evidence: |
| GO:0019900 kinase binding | IPI PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | KEEP AS NON CORE | Summary: EGFR physically associates with the lipid kinase DGKQ. Reason: The source abstract explicitly reports physical association of EGFR with DGK-theta, and the exact imported accession P52824 is DGKQ. Its official catalytic record establishes phosphorylation of diacylglycerol, so the existing kinase-binding class is appropriate. It would be incorrect to refine this association to protein-kinase binding merely because both partners are called kinases. The original full Methods were unavailable. Supporting Evidence: |
| 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 participates in PKC-dependent signaling and feedback in A431 cells. Reason: The complete abstract reports EGF-induced, PKC-dependent EGFR Thr654 phosphorylation and shows that EGFR activation is required for the DGK-theta trafficking response within this pathway. This supports the curated positive PKC-signaling context while retaining the negative feedback of DGK-theta/PKC on receptor tyrosine phosphorylation as a distinct observation. It does not assign PKC catalysis to EGFR; detailed original controls were unavailable. Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IMP PMID:18483258 UVA-induced cell cycle progression is mediated by a disinteg... | ACCEPT | Summary: EGFR signaling mediates the measured keratinocyte UVA response. Reason: The available article text reports low, nonlethal UVA exposure in human HaCaT keratinocytes, EGFR/AKT activation and cyclin D1 induction, with EGFR inhibition and upstream ADAM17 perturbation. Its retained abstract and Discussion contain these positive results, although the cached text omits the operative Methods and Results sections. This supports the existing receptor pathway in this transactivation context; it is not evidence that EGFR directly senses photons. Supporting Evidence: |
| 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: PI3K/AKT is a supported downstream signaling context. Reason: The available article text reports low, nonlethal UVA exposure in human HaCaT keratinocytes, EGFR/AKT activation and cyclin D1 induction, with EGFR inhibition and upstream ADAM17 perturbation. Its retained abstract and Discussion contain these positive results, although the cached text omits the operative Methods and Results sections. Retain this downstream process without transferring PI3K or AKT catalytic activity to EGFR. Supporting Evidence: |
| 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: The measured EGFR-dependent response promotes G1/S progression. Reason: The available article text reports low, nonlethal UVA exposure in human HaCaT keratinocytes, EGFR/AKT activation and cyclin D1 induction, with EGFR inhibition and upstream ADAM17 perturbation. Its retained abstract and Discussion contain these positive results, although the cached text omits the operative Methods and Results sections. The cyclin D1 and cell-cycle findings support a context-dependent proliferative output, not EGFR performing cell-cycle machinery chemistry. Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | ACCEPT | Summary: EGFR signaling contributes to the endothelial barrier response examined with SH3GL2. Reason: The source abstract reports EGFR/ERK activation in human hCMEC/D3 brain endothelial cells after SH3GL2 perturbation, with EGFR and pathway inhibition affecting the barrier response. This establishes a receptor-signaling context; it does not equate EGFR with a tight-junction structural component. Original full Methods were unavailable. Supporting Evidence: |
| GO:0043410 positive regulation of MAPK cascade | IDA PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | KEEP AS NON CORE | Summary: EGFR promotes ERK pathway signaling in the SH3GL2 endothelial model. Reason: The complete abstract links SH3GL2 manipulation to EGFR phosphorylation and downstream ERK activation and reports inhibitor-sensitive barrier effects. Positive regulation of the MAPK cascade is retained as a contextual signaling output. The paper does not thereby establish direct EGFR phosphorylation of a MAP kinase kinase. Supporting Evidence: |
| GO:0005794 Golgi apparatus | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human Protein Atlas imaging supports a Golgi-associated EGFR pool. Reason: The EGFR subcellular page assigns Golgi apparatus supported reliability and reports this pattern with CAB080474, CAB080508 and CAB080513 in several human cell lines, as well as HPA018530 in ASC52telo. This is positive antibody-localization evidence for a cellular pool; it is not inferred solely from secretory-pathway transit. The source does not establish a distinct Golgi molecular function or resolve which natural product accounts for the signal. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0005829 cytosol | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: The source reports cytosolic EGFR immunoreactivity in a specific ciliated-cell assay. Reason: HPA018530 staining in human RPTEC/TERT1 cells is annotated as cytosol together with plasma membrane and primary cilium. Cytosol is absent from the current gene-level summary but remains a positive assay-level observation. Retain that bounded observation without treating the cytoplasmic kinase domain of a membrane receptor as proof of a soluble cytosolic protein pool. The assay does not identify the molecular species responsible for this signal. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: Multiple human-cell assays directly support plasma-membrane EGFR localization. Reason: The Human Protein Atlas assigns supported reliability to the plasma-membrane location and records membrane staining with several antibodies in A-431, U-251MG, HeLa, MCF-7, U2OS and other human cells. This source supports the receptor compartment directly and is consistent with its ligand-dependent surface signaling. It does not imply exclusive residence at the surface. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0005929 cilium | IDA GO_REF:0000052 | UNDECIDED | Summary: The reported primary-cilium signal remains uncertain at the source level. Reason: HPA018530 staining is annotated at primary cilia in human RPTEC/TERT1 and serum-starved hTERT-RPE1 cells, with single-cell variation. The location-specific reliability is uncertain even though the overall EGFR subcellular score is supported. This positive observation is preserved, but the available antibody-based evidence does not resolve whether it establishes the gene-specific ciliary pool. Uncertainty is not a claim that EGFR cannot localize to cilia. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0030054 cell junction | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human-cell imaging supports EGFR at cell junctions. Reason: The Human Protein Atlas gives cell junctions supported reliability and reports the location with HPA018530 and CAB000035 in A-431 cells and with CAB000035 in U-251MG cells. Retain this specific membrane-associated pool without inferring junction assembly or adhesion activity from localization alone. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0036064 ciliary basal body | IDA GO_REF:0000052 | UNDECIDED | Summary: The basal-body observation has unresolved location-specific reliability. Reason: The human serum-starved hTERT-RPE1 assay with HPA018530 reports basal-body staining with single-cell variation, but the source rates the basal-body location uncertain. Its overall supported score cannot substitute for this location-specific assessment. Preserve the observation and its uncertainty without asserting absence from basal bodies or transferring basal-body assembly activity to EGFR. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0097225 sperm midpiece | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human sperm imaging reports EGFR immunoreactivity in the midpiece. Reason: The Human Protein Atlas sperm assay uses HPA018530 on human sperm from a healthy donor and annotates the midpiece along with other flagellar regions and the plasma membrane. The corresponding location has approved reliability. This supports a source-specific sperm pool, while the antibody assay does not establish a motility mechanism, a specific natural product, or universal localization across sperm states. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0097228 sperm principal piece | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human sperm imaging reports EGFR immunoreactivity in the principal piece. Reason: The Human Protein Atlas sperm assay uses HPA018530 on human sperm from a healthy donor and annotates the principal piece along with other flagellar regions and the plasma membrane. The corresponding location has approved reliability. This supports a source-specific sperm pool, while the antibody assay does not establish a motility mechanism, a specific natural product, or universal localization across sperm states. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0097229 sperm end piece | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human sperm imaging reports EGFR immunoreactivity in the end piece. Reason: The Human Protein Atlas sperm assay uses HPA018530 on human sperm from a healthy donor and annotates the end piece along with other flagellar regions and the plasma membrane. The corresponding location has approved reliability. This supports a source-specific sperm pool, while the antibody assay does not establish a motility mechanism, a specific natural product, or universal localization across sperm states. Supporting Evidence: GO_REF:0000052 https://www.proteinatlas.org/ENSG00000146648-EGFR/subcellular |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-177934 | MODIFY | Summary: Refine to epidermal growth factor receptor activity in the explicit EGFR catalytic context. Reason: In R-HSA-177934 (EGFR autophosphorylation), the captured typed path 177934 --catalystActivity--> 9624430; 9624430 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The catalyst activity matches the imported kinase term and explicitly identifies EGFR as activeUnit. In this ligand-activated membrane-receptor context, the existing EGFR receptor activity is the more informative integrated activity; the catalytic reaction is not inferred from membership in another enzyme's complex. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: Reactome:R-HSA-177934 |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-182969 | MODIFY | Summary: Refine to epidermal growth factor receptor activity in the explicit EGFR catalytic context. Reason: In R-HSA-182969 (Phosphorylation of CBL (EGFR:CBL)), the captured typed path 182969 --catalystActivity--> 183047; 183047 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The catalyst activity matches the imported kinase term and explicitly identifies EGFR as activeUnit. In this ligand-activated membrane-receptor context, the existing EGFR receptor activity is the more informative integrated activity; the catalytic reaction is not inferred from membership in another enzyme's complex. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: Reactome:R-HSA-182969 |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-183058 | MODIFY | Summary: Refine to epidermal growth factor receptor activity in the explicit EGFR catalytic context. Reason: In R-HSA-183058 (Phosphorylation of CBL (EGFR:GRB2:CBL)), the captured typed path 183058 --catalystActivity--> 182979; 182979 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The catalyst activity matches the imported kinase term and explicitly identifies EGFR as activeUnit. In this ligand-activated membrane-receptor context, the existing EGFR receptor activity is the more informative integrated activity; the catalytic reaction is not inferred from membership in another enzyme's complex. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: Reactome:R-HSA-183058 |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-212710 | MODIFY | Summary: Refine to epidermal growth factor receptor activity in the explicit EGFR catalytic context. Reason: In R-HSA-212710 (EGFR activates PLC-gamma1 by phosphorylation), the captured typed path 212710 --catalystActivity--> 212705; 212705 --activeUnit--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The catalyst activity matches the imported kinase term and explicitly identifies EGFR as activeUnit. In this ligand-activated membrane-receptor context, the existing EGFR receptor activity is the more informative integrated activity; the catalytic reaction is not inferred from membership in another enzyme's complex. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: Reactome:R-HSA-212710 |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-8867041 | MODIFY | Summary: Refine to epidermal growth factor receptor activity in the explicit EGFR catalytic context. Reason: In R-HSA-8867041 (EGFR phosphorylates EPS15), the captured typed path 8867041 --catalystActivity--> 8867039; 8867039 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The catalyst activity matches the imported kinase term and explicitly identifies EGFR as activeUnit. In this ligand-activated membrane-receptor context, the existing EGFR receptor activity is the more informative integrated activity; the catalytic reaction is not inferred from membership in another enzyme's complex. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: Reactome:R-HSA-8867041 |
| GO:0005515 protein binding | IPI PMID:15611079 Epigen, the last ligand of ErbB receptors, reveals intricate... | MODIFY | Summary: EGFR binds the growth factor epigen. Reason: The complete source abstract describes recombinant epigen binding and mitogenic activity through ERBB1/EGFR, with substantially lower affinity than EGF. The official Q6UW88 identity and growth-promoting function support growth factor binding. Epigen is not relabeled as EGF, and no exact mature-fragment boundary or native-product equivalence is inferred from the unavailable full Methods. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:12828935 Activation of epidermal growth factor receptor signals induc... | ACCEPT | Summary: EGFR signaling regulates the astrocyte NOS2 response. Reason: The source abstract reports EGFR activation in human optic-nerve-head astrocytes and its requirement for NOS2 induction under the investigated pressure-related conditions. This is a positive receptor-signaling contribution rather than evidence that EGFR itself performs nitric-oxide synthesis. Detailed original Methods were unavailable. Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IMP PMID:17655843 EGF receptor transactivation and PI3-kinase mediate stimulat... | ACCEPT | Summary: EGFR transactivation participates in the receptor signaling pathway in the tested intestinal-cell system. Reason: The authentic abstract reports that EGFR inhibition or desensitization attenuates UK14304-induced ERK and Akt phosphorylation in CaCo2-3B cells. HB-EGF neutralization and MMP blockade also attenuate the response. This is positive support for the curated IMP assertion and a central receptor-signaling role. The human transgene identified in the abstract is alpha2A-adrenoreceptor; an EGFR transgene or a particular EGFR isoform was not established. Full Methods and Results remain unavailable. Supporting Evidence: |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | IMP PMID:17655843 EGF receptor transactivation and PI3-kinase mediate stimulat... | ACCEPT | Summary: EGFR signaling positively regulates the PI3KβAkt pathway in the tested transactivation response. Reason: The abstract directly reports Akt phosphorylation that is attenuated by EGFR inhibition or desensitization and by PI3K inhibitors in CaCo2-3B cells. This supports the signed curated process. Being downstream of receptor activation does not make this major signaling output non-core. The result does not establish direct EGFR catalysis of Akt phosphorylation, a defined EGFR isoform, or an in vivo intestinal-repair mechanism; operative full text was not recovered. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177935 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177935 (SHP2 dephosphorylates Tyr 992 on EGFR), the captured typed path 177935 --input--> 180269; 180269 --hasComponent--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177935 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8863804 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8863804 (PTPN12 dephosphorylates ERBB2 on tyrosine Y1248), the captured typed path 8863804 --input--> 1963588; 1963588 --hasMember--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8863804 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864029 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8864029 (PTPN12 dephosphorylates EGFR at Y1172 (Y1148)), the captured typed path 8864029 --input--> 179882; 179882 --hasComponent--> 179860; 179860 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8864029 |
| 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-dependent signaling supports miR-221/222 expression in the basal-like breast-cancer context. Reason: The authentic abstract reports reduced miR-221/222 abundance after EGFR or MEK inhibition and identifies FOSL1 as the transcriptional activator. Retain the curator-supported positive transcription assertion as a context-specific transcriptional response, without attributing promoter binding to EGFR. The abstract alone does not separate every transcription-versus-RNA-abundance assay; full Methods and Results could not be recovered. This limitation does not contradict the imported IMP annotation. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:15611079 Epigen, the last ligand of ErbB receptors, reveals intricate... | ACCEPT | Summary: The epigen study examines cell-surface EGFR ligand responses. Reason: The abstract reports ligand binding, receptor-mediated ligand depletion and receptor down-regulation in cells expressing ERBB1/EGFR. These are consistent with the established plasma-membrane receptor pool. The original full Methods were unavailable, so no specific assay-cell species or expression-construct sequence is asserted. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:2472218 EGF induces tyrosine phosphorylation of phospholipase C-II: ... | MODIFY | Summary: The PLC-II response supports ligand-dependent EGFR receptor signaling. Reason: The verified abstract reports rapid EGF-induced PLC-II tyrosine phosphorylation, reciprocal recovery of PLC-II and EGFR in immune complexes, and inhibition of the response by an EGFR kinase inhibitor. The integrated epidermal growth factor receptor activity term better represents this ligand-responsive cellular evidence than isolated protein tyrosine kinase activity. The operative full article was not recovered, so this is not described as a personally verified purified EGFR-to-PLC-II phosphotransfer assay. The source does not establish activity of naturally truncated receptor products. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR binds EGF and activates receptor signaling in the HeLa dynamin experiment. Reason: The original Methods and Results measure surface EGF binding, ligand-dependent EGFR tyrosine phosphorylation and receptor internalization in human HeLa cells with regulated dynamin K44A expression. These are receptor-function measurements; altered EGF affinity and altered endocytosis are not conflated with receptor abundance or intrinsic affinity in every condition. Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF recep... | ACCEPT | Summary: The source examines EGFR receptor constructs and their phosphorylation-dependent effector docking. Reason: The complete original tests wild-type and mutant receptors from transfected NIH3T3 cells, alongside a baculovirus-produced intracellular domain. These experiments are compatible with the established receptor function. The isolated intracellular preparation and kinase-negative mutant are not described as complete ligand-responsive natural products. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR occupies the cell surface in the EGF-binding and internalization experiment. Reason: The original radioligand binding and acid-wash internalization experiments distinguish surface-bound from internalized EGF in HeLa cells. Membrane-impermeable crosslinking and surface-receptor measurements support plasma-membrane localization. The source does not claim that the receptor remains exclusively at the surface. Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:9890893 Identification of tyrosine phosphorylation sites in human Ga... | ACCEPT | Summary: EGFR phosphorylates a docking protein within its signaling pathway. Reason: The complete source abstract reports direct phosphorylation of recombinant human GAB1 by WGA-purified EGFR and a recombinant receptor kinase domain, followed by phosphosite mapping and phosphotyrosine-dependent recruitment of Syp. This establishes an active signaling step. Unavailable full Methods do not justify additional construct-species or native stoichiometry claims. Supporting Evidence: |
| GO:0038134 ERBB2-EGFR signaling pathway | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR participates in signaling with ERBB2 in the measured heterodimer context. Reason: The original reciprocal immunoprecipitation experiments recover a small preformed EGFRβERBB2 heterodimer population, and EGF stimulates the ERBB2 Tyr1248 activation readout. The paper explicitly separates this heterodimer behavior from the high-affinity EGF-binding effect of dynamin perturbation. It does not show that every heterodimer forms only after ligand addition. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27872189 Biophysical Evidence for Intrinsic Disorder in the C-termina... | MODIFY | Summary: A phosphorylated EGFR tail binds the isolated GRB2 SH2 domain. Reason: PMID:27872189 directly compares GST-GRB2 SH2 binding to phosphorylated and unphosphorylated EGFR carboxy-terminal tail, with GST control. The operative Methods describe human EGFR intracellular and kinase constructs expressed in Sf9 cells and a separately produced tail. This is evidence for the actual SH2 interface, rather than an inference from a domain present in an intact partner. Published mature-protein and reference numbering conventions remain distinct; the fragment assay does not establish equivalent binding by all natural EGFR products. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:9890893 Identification of tyrosine phosphorylation sites in human Ga... | ACCEPT | Summary: The GAB1 experiment directly supports protein tyrosine kinase activity. Reason: The source abstract describes cell-free phosphorylation of recombinant human GAB1 by two EGFR preparations and identifies tyrosine phosphosites by sequencing and mass spectrometry. The receptor kinase-domain preparation is not a complete ligand-responsive receptor, so the measured catalytic term is retained rather than automatically replaced by receptor activity. Supporting Evidence: |
| GO:0030296 protein tyrosine kinase activator activity | IDA PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF recep... | ACCEPT | Summary: EGFR has allosteric tyrosine-kinase activator activity, distinct from phosphorylation-dependent effector docking. Reason: The gene-level activator claim is supported independently by PMID:16777603: complementary asymmetric-interface mutants and kinase-dead controls establish that one human EGFR kinase domain can allosterically activate its partner. These experiments use purified kinase domains and engineered full-length receptors, not every natural EGFR product. The original PMID:2176151 remains evidence for trans-phosphorylation restoring GAP/PLC-gamma docking to kinase-negative EGFR; it does not demonstrate restoration of that mutantβs catalytic activity or an ERBB2 activation experiment. Acceptance of the activator function therefore does not recast the docking experiment as catalytic activation. |
| GO:0030296 protein tyrosine kinase activator activity | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR contributes to ERBB2 activation in the receptor heterodimer. Reason: The original Figure 5 and Results measure EGF-induced ERBB2 Tyr1248 phosphorylation as its activation readout, while reciprocal co-immunoprecipitation establishes an EGFRβERBB2 heterodimer population. This supports the curated tyrosine-kinase activator function at the cellular heterodimer level. The experiment is not a purified allosteric-interface assay and does not resolve which kinase directly supplies every phosphate. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:11331309 Real time fluorescence imaging of PLC gamma translocation an... | ACCEPT | Summary: Tagged EGFR imaging directly establishes its plasma-membrane pool. Reason: The source follows EGFR-GFP/RFP in COS7 and A431 cellular systems before and after EGF. Plasma-membrane receptor signal is directly described together with subsequent internalization. The construct route and checked PCR fragments do not authenticate one of the present natural alternative products. Supporting Evidence: |
| GO:0032587 ruffle membrane | IDA PMID:11331309 Real time fluorescence imaging of PLC gamma translocation an... | KEEP AS NON CORE | Summary: EGFR is observed at EGF-induced membrane ruffles in the imaging assay. Reason: The original fluorescence-imaging results describe receptor-bearing membrane ruffles following EGF stimulation. This supports the specialized membrane pool under the assay conditions. It does not require a claim that the paper independently measured cell migration or that ruffle localization is universal. Supporting Evidence: |
| GO:0097708 intracellular vesicle | IDA PMID:11331309 Real time fluorescence imaging of PLC gamma translocation an... | MODIFY | Summary: The reported internalized receptor vesicles are endosomes. Reason: After EGF stimulation, the source describes EGFR-positive intracellular vesicles that enlarge and fuse, identifying the migrating structures at approximately15minutes as endosomes in the context of the prior trafficking study. Endosome specifies this observed internalized receptor pool more informatively than intracellular vesicle. The claim does not require that all PLC-gamma-positive vesicles contain EGFR or that these data establish a particular endosomal subcompartment. Proposed replacements: endosome Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17334392 A crucial role of plasma membrane-associated sialidase in th... | UNDECIDED | Summary: The source-specific EGFRβNEU3 physical-association claim remains unresolved. Reason: The authentic PMID:17334392 abstract reports NEU3 depletion or overexpression in human cancer cells and changes in EGFR phosphorylation and downstream signaling. The operative original binding experiment was not recovered through the publisher routes. Those functional effects alone do not establish a physical pair, although the curated IPI assertion remains credible and is preserved. NEU3 enzyme identity does not resolve this source-specific assay gap; the record is left undecided without claiming that the proteins cannot associate. Supporting Evidence: |
| GO:0019900 kinase binding | IPI PMID:18722344 BCAR3 regulates EGF-induced DNA synthesis in normal human br... | UNDECIDED | Summary: The source-specific kinase-binding assignment has an unresolved partner mismatch. Reason: The imported partner P46108 is the noncatalytic adaptor CRK, not a protein kinase. The available abstract positively reports BCAR3 association with activated EGFR, but the full Methods were unavailable and do not resolve why this source carries the CRK-linked kinase-binding assertion. The source object is preserved; neither a false experiment nor an alternate assayed partner is invented. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26988023 Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facil... | KEEP AS NON CORE | Summary: EGFR associates with the heme-dependent PGRMC1 complex. Reason: PMID:26988023 reports tagged PGRMC1βEGFR coimmunoprecipitation in HCT116 cells and an in vitro assay combining purified PGRMC1 cytosolic region with commercial full-length EGFR isolated from human A431 cells. Heme, PGRMC1 Y113F and carbon-monoxide manipulations distinguish conditions of association. PGRMC1 heme handling and regulation of other enzymes do not establish that it is itself a catalytic enzyme or a steroid receptor. Retain the positive protein-binding assertion with the actual fragment and preparation limits; no natural-product equivalence or universal heme requirement is inferred. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25187647 Structural basis for activation of trimeric Gi proteins by m... | MODIFY | Summary: EGFR binds GIV in a complex that connects the receptor to G-alpha-i. Reason: The operative PMID:25187647 experiments demonstrate binding of GIV carboxy-terminal material to phosphorylated EGFR tail and assembly of a ternary complex with purified G-alpha-i3. Separate GIV SH2-like and GEF-motif mutations disrupt the corresponding interactions, with cellular complementation providing a distinct assay. This independently measured tethering of signaling components supports scaffold-protein binding. The GEF role is not treated as catalytic enzyme activity, and a modeled SH2-like fold is not silently equated to an isolated canonical SH2-domain assay. The exact fragments and engineered mutants are not natural EGFR products. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18722344 BCAR3 regulates EGF-induced DNA synthesis in normal human br... | MODIFY | Summary: EGFR associates with the SH2 domain of BCAR3. Reason: The complete abstract reports direct BCAR3 association with activated EGFR and SH2-dependent signaling. The official O75815 SUBUNIT assessment specifically maps EGFR association to the BCAR3 SH2 domain with this PMID. Together these support SH2 domain binding, while the inaccessible original Methods leave detailed construct and assay conditions unresolved. No controversial BCAR3 GEF activity is transferred to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20462955 A G{alpha}i-GIV molecular complex binds epidermal growth fac... | MODIFY | Summary: The measured GIV association supports cytoskeletal regulatory protein binding. Reason: The source reports EGFRβGIV association in cells and binding between purified GIV C-terminal protein and a phosphorylated EGFR-tail preparation. Human GIV/CCDC88A (Q3V6T2) regulates actin organization, including stress-fiber and lamellipodium formation, so GO:0005519 describes the verified partner class. This does not assign GIV guanine-nucleotide exchange or actin-regulatory activity to EGFR. The article gives differing fragment endpoints in Methods and captions (EGFR1046β1210 versus1064β1210; GIV1623β1870 versus1660β1870), which are retained as construct limits rather than silently harmonized. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | KEEP AS NON CORE | Summary: EGFR physically associates with SH3GL2/endophilin-A1 in the reported endothelial assay. Reason: The complete abstract explicitly reports co-immunoprecipitation and colocalization of EGFR with SH3GL2 in human brain endothelial cells. The official Q99962 record describes membrane-curvature and endocytic scaffold functions rather than a demonstrated enzyme class. This supports generic binding under the project-specific policy, without assuming a mapped SH3-domain contact or a purified binary interface from the unavailable full Methods. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | IMP PMID:24854121 Endophilin-1 regulates blood-brain barrier permeability by c... | UNDECIDED | Summary: The source-specific perinuclear localization assertion remains unresolved. Reason: The complete abstract supports EGFRβSH3GL2 association and signaling in human brain endothelial cells, but does not resolve the perinuclear localization experiment. The original body and imaging details were not recovered. The annotation is therefore left undecided; absence of a compartment description from the abstract is not evidence that the observation was false. Supporting Evidence: |
| GO:0045121 membrane raft | ISS GO_REF:0000024 | ACCEPT | Summary: Raft association has a literal bovine experimental donor. Reason: Current F1N7F3 is bovine EGFR, not rat or mouse. Its exact GO:0045121 IDA cites PMID:28833817. The complete abstract explicitly reports raft and non-raft fractionation and EGFR-containing immunoprecipitates from ouabain-capacitated bovine sperm, supporting the positive donor localization. Preserve the human ISS as a conserved receptor membrane pool, while stating that this donor study is not a human-sperm assay or proof of exclusive raft residence. Full publisher text was inaccessible in this bounded attempt; no missing figure or construct detail is invented. |
| GO:0051117 ATPase binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The donor identifies an ATP1A4-associated EGFR pool. Reason: The current bovine F1N7F3 IPI record and PMID:28833817 abstract identify immunoprecipitation association of EGFR with the Na/K ATPase ATP1A4 in raft and non-raft sperm fractions. This supports binding to an ATPase-class partner without requiring a purified binary interface. It does not establish that human EGFR has ATPase catalytic activity, that every ATPase associates, or that the observed complex is a separate core receptor mechanism. Publisher full-text access failed; retain the explicitly positive abstract-level assay scope. |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868658 | ACCEPT | Summary: Retain clathrin-coated endocytic vesicle membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868658 (HSPA8-mediated ATP hydrolysis promotes vesicle uncoating), the captured typed path 8868658 --input--> 8868627; 8868627 --hasComponent--> 8868710; 8868710 --hasMember--> 8869200; 8869200 --hasComponent--> 8869164; 8869164 --hasMember--> 8935905; 8935905 --hasComponent--> 8869138 reaches human EGFR entity 8869138 (p-6Y-EGFR [clathrin-coated endocytic vesicle membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0030669; this location is not inferred solely from the event compartment. This is the internalized receptor cargo pool; coat assembly, HSPA8 ATPase and dynamin GTPase activities remain functions of their respective proteins. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868658 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868659 | ACCEPT | Summary: Retain clathrin-coated endocytic vesicle membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868659 (Clathrin recruits auxilins to the clathrin-coated vesicle), the captured typed path 8868659 --input--> 8868624; 8868624 --hasComponent--> 8868710; 8868710 --hasMember--> 8869200; 8869200 --hasComponent--> 8869164; 8869164 --hasMember--> 8935905; 8935905 --hasComponent--> 8869138 reaches human EGFR entity 8869138 (p-6Y-EGFR [clathrin-coated endocytic vesicle membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0030669; this location is not inferred solely from the event compartment. This is the internalized receptor cargo pool; coat assembly, HSPA8 ATPase and dynamin GTPase activities remain functions of their respective proteins. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868659 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868660 | ACCEPT | Summary: Retain clathrin-coated endocytic vesicle membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868660 (Auxilin recruits HSPA8:ATP to the clathrin-coated vesicle), the captured typed path 8868660 --input--> 8868626; 8868626 --hasComponent--> 8868710; 8868710 --hasMember--> 8869200; 8869200 --hasComponent--> 8869164; 8869164 --hasMember--> 8935905; 8935905 --hasComponent--> 8869138 reaches human EGFR entity 8869138 (p-6Y-EGFR [clathrin-coated endocytic vesicle membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0030669; this location is not inferred solely from the event compartment. This is the internalized receptor cargo pool; coat assembly, HSPA8 ATPase and dynamin GTPase activities remain functions of their respective proteins. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868660 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8868661 | ACCEPT | Summary: Retain clathrin-coated endocytic vesicle membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868661 (Dynamin-mediated GTP hydrolysis promotes vesicle scission), the captured typed path 8868661 --output--> 8868624; 8868624 --hasComponent--> 8868710; 8868710 --hasMember--> 8869200; 8869200 --hasComponent--> 8869164; 8869164 --hasMember--> 8935905; 8935905 --hasComponent--> 8869138 reaches human EGFR entity 8869138 (p-6Y-EGFR [clathrin-coated endocytic vesicle membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0030669; this location is not inferred solely from the event compartment. This is the internalized receptor cargo pool; coat assembly, HSPA8 ATPase and dynamin GTPase activities remain functions of their respective proteins. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868661 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8869438 | ACCEPT | Summary: Retain clathrin-coated endocytic vesicle membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8869438 (Dissociation of clathrin-associated proteins), the captured typed path 8869438 --output--> 8868710; 8868710 --hasMember--> 8869200; 8869200 --hasComponent--> 8869164; 8869164 --hasMember--> 8935905; 8935905 --hasComponent--> 8869138 reaches human EGFR entity 8869138 (p-6Y-EGFR [clathrin-coated endocytic vesicle membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0030669; this location is not inferred solely from the event compartment. This is the internalized receptor cargo pool; coat assembly, HSPA8 ATPase and dynamin GTPase activities remain functions of their respective proteins. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8869438 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8871193 | ACCEPT | Summary: Retain clathrin-coated endocytic vesicle membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8871193 (Dissociation of AAK1 and dephosphorylation of AP-2 mu2), the captured typed path 8871193 --input--> 8871149; 8871149 --hasComponent--> 8868620; 8868620 --hasComponent--> 8868710; 8868710 --hasMember--> 8869200; 8869200 --hasComponent--> 8869164; 8869164 --hasMember--> 8935905; 8935905 --hasComponent--> 8869138 reaches human EGFR entity 8869138 (p-6Y-EGFR [clathrin-coated endocytic vesicle membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0030669; this location is not inferred solely from the event compartment. This is the internalized receptor cargo pool; coat assembly, HSPA8 ATPase and dynamin GTPase activities remain functions of their respective proteins. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8871193 |
| GO:0030669 clathrin-coated endocytic vesicle membrane | TAS Reactome:R-HSA-8871194 | ACCEPT | Summary: Retain clathrin-coated endocytic vesicle membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8871194 (RAB5 and GAPVD1 bind AP-2), the captured typed path 8871194 --input--> 8868620; 8868620 --hasComponent--> 8868710; 8868710 --hasMember--> 8869200; 8869200 --hasComponent--> 8869164; 8869164 --hasMember--> 8935905; 8935905 --hasComponent--> 8869138 reaches human EGFR entity 8869138 (p-6Y-EGFR [clathrin-coated endocytic vesicle membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0030669; this location is not inferred solely from the event compartment. This is the internalized receptor cargo pool; coat assembly, HSPA8 ATPase and dynamin GTPase activities remain functions of their respective proteins. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8871194 |
| GO:0005737 cytoplasm | IDA PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | MODIFY | Summary: The source resolves the intracellular EGFR pool as endosomal. Reason: In human HeLa cells, EGFR leaves the cell surface after EGF stimulation and is reported in early endosomes; ANKRD13 overexpression delays this redistribution rather than eliminating it. The Figure7 text also reports internalization after1hour in transfected cells. Endosome is therefore more informative than undifferentiated cytoplasm. This inference uses the receptor distribution, not merely the presence of its cytoplasmic kinase domain or ANKRD13 in the cytoplasm. Proposed replacements: endosome Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | ACCEPT | Summary: The ANKRD13 study directly detects cell-surface EGFR. Reason: EGFR staining and the surface-receptor measurements in human HeLa cells establish the plasma-membrane pool before EGF stimulation and its retention when ANKRD13A/B/D are overexpressed. The observed pool is compatible with subsequent endosomal trafficking and does not imply permanent surface residence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | KEEP AS NON CORE | Summary: Retain the measured EGFRβANKRD13D association with its ubiquitin-dependent mechanism. Reason: The study reports EGF-dependent association of ubiquitinated EGFR with transfected ANKRD13A/B/D in human HeLa cells. Endogenous ANKRD13A/D association was also detected. The ANKRD13 UIMs recognize the ubiquitin moiety on EGFR, and a stripped-receptor assay separates this from associated cellular proteins. These findings support the imported protein-association assertion but do not establish binding to an ankyrin repeat or give EGFR ubiquitin-binding activity. No informative partner-class refinement is established by the saved class records, so the supported generic term is retained under the project-specific policy. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1169421 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1169421 (Trans-autophosphorylation of activated ligand-responsive EGFR mutant dimers), the captured typed path 1169421 --output--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1169421 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1218833 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1218833 (Binding of ligand-responsive EGFR mutants to chaperoning proteins HSP90 and CDC37), the captured typed path 1218833 --input--> 1182966; 1182966 --hasMember--> 1176052; 1176052 --hasMember--> 1169418 reaches human EGFR entity 1169418 (EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1218833 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220610 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1220610 (Non-covalent tyrosine kinase inhibitors bind and inactivate sensitive ligand-responsive EGFR cancer mutants), the captured typed path 1220610 --output--> 1220585; 1220585 --hasMember--> 1220574; 1220574 --hasComponent--> 1220573; 1220573 --hasComponent--> 1182967; 1182967 --hasMember--> 1181386 reaches human EGFR entity 1181386 (EGFR L858R;T790M [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1220610 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220612 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1220612 (Binding of EGF to ligand-responsive EGFR mutants), the captured typed path 1220612 --input--> 1218825; 1218825 --hasMember--> 1220583; 1220583 --hasComponent--> 1176052; 1176052 --hasMember--> 1169418 reaches human EGFR entity 1169418 (EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1220612 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220613 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1220613 (EGF-induced dimerization of ligand-responsive EGFR mutants), the captured typed path 1220613 --input--> 1220578; 1220578 --hasMember--> 1220580; 1220580 --hasComponent--> 1176052; 1176052 --hasMember--> 1169418 reaches human EGFR entity 1169418 (EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1220613 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220614 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1220614 (Spontaneous dimerization of ligand-responsive EGFR mutants), the captured typed path 1220614 --input--> 1218825; 1218825 --hasMember--> 1220583; 1220583 --hasComponent--> 1176052; 1176052 --hasMember--> 1169418 reaches human EGFR entity 1169418 (EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1220614 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225947 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225947 (Binding of SHC1 to p-6Y-EGFR mutants), the captured typed path 1225947 --input--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225947 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225949 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225949 (Binding of CBL to ligand-responsive p-6Y-EGFR mutants), the captured typed path 1225949 --input--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225949 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225950 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225950 (Binding of GRB2:SOS1 complex to phosphorylated ligand-responsive EGFR mutants), the captured typed path 1225950 --input--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225950 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225951 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225951 (SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with ligand-responsive p-6Y-EGFR mutants)), the captured typed path 1225951 --catalystActivity--> 1225931; 1225931 --physicalEntity--> 1225859; 1225859 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225951 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225952 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225952 (Phosphorylation of SHC1 by ligand-responsive p-6Y-EGFR mutants), the captured typed path 1225952 --input--> 1225858; 1225858 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225952 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225956 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225956 (Inefficient ubiquitination of ligand-responsive p-6Y-EGFR mutants by p-Y371-CBL), the captured typed path 1225956 --input--> 1225857; 1225857 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. The FailedReaction describes deficient mutant binding or ubiquitination, not absence of the membrane-localized receptor. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225956 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225957 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225957 (SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and ligand-responsive p-6Y-EGFR mutants)), the captured typed path 1225957 --catalystActivity--> 1225930; 1225930 --physicalEntity--> 1225856; 1225856 --hasComponent--> 1225854; 1225854 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225957 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225960 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225960 (Phosphorylation of CBL by ligand-responsive p-6Y-EGFR mutants), the captured typed path 1225960 --input--> 1225855; 1225855 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225960 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225961 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225961 (Phosphorylated SHC1 in complex with ligand-responsive p-6Y-EGFR mutants recruits GRB2:SOS1 complex), the captured typed path 1225961 --input--> 1225854; 1225854 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225961 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1226012 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1226012 (Binding of PI3K to complex of GRB2:GAB1 and ligand-responsive p-6Y-EGFR mutants), the captured typed path 1226012 --input--> 1226015; 1226015 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1226012 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1226014 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1226014 (Conversion of PIP2 to PIP3 by PI3K bound to ligand-responsive p-6Y-EGFR mutants), the captured typed path 1226014 --catalystActivity--> 1226011; 1226011 --physicalEntity--> 1226013; 1226013 --hasComponent--> 1226015; 1226015 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1226014 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1226016 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1226016 (Binding of GRB2:GAB1 complex to ligand-responsive p-6Y-EGFR mutants), the captured typed path 1226016 --input--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1226016 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247841 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1247841 (PLCG1 binds to ligand-responsive p-6Y-EGFR mutants), the captured typed path 1247841 --input--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1247841 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247842 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1247842 (Dissociation of phosphorylated PLCG1 from ligand-responsive p-6Y-EGFR mutants), the captured typed path 1247842 --output--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1247842 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247844 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1247844 (Phosphorylation of PLCG1 by ligand-responsive p-6Y-EGFR mutants), the captured typed path 1247844 --input--> 1247845; 1247845 --hasComponent--> 1181062; 1181062 --hasMember--> 1220652; 1220652 --hasComponent--> 1220648; 1220648 --hasMember--> 1809167; 1809167 --hasComponent--> 1182977; 1182977 --hasMember--> 1169417 reaches human EGFR entity 1169417 (p-6Y-EGFR G719S [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1247844 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1220611 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1220611 (Covalent tyrosine kinase inhibitors bind and inactivate EGFR kinase domain mutant dimers resistant to non-covalent tyrosine kinase inhibitors), the captured typed path 1220611 --input--> 1220585; 1220585 --hasMember--> 1220574; 1220574 --hasComponent--> 1220573; 1220573 --hasComponent--> 1182967; 1182967 --hasMember--> 1181386 reaches human EGFR entity 1181386 (EGFR L858R;T790M [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1220611 |
| GO:0019903 protein phosphatase binding | IPI PMID:28759036 Deficiency in VHR/DUSP3, a suppressor of focal adhesion kina... | UNDECIDED | Summary: The particular citation does not yet resolve EGFR binding to DUSP3/VHR. Reason: PMID:28759036 has a verified abstract describing VHR effects on focal-adhesion signaling and increased EGFR phosphorylation after VHR loss. The operative original pair-association experiment was inaccessible in the bounded source check. DUSP3 is a protein phosphatase, but a phosphorylation response does not itself verify binding. Preserve the experimental source and correct partner identity with uncertainty about this citation, rather than removing the annotation or inferring nonbinding from its FAK-focused title. Supporting Evidence: |
| GO:0010008 endosome membrane | TAS Reactome:R-HSA-9611147 | ACCEPT | Summary: Retain endosome membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9611147 (Endocytic Uptake of HCMV Virion), the captured typed path 9611147 --output--> 9611144; 9611144 --hasMember--> 9611160 reaches human EGFR entity 9611160 (EGFR [endosome membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0010008; this location is not inferred solely from the event compartment. The membrane location is specifically on the endosomal output EGFR entity, although the event's own compartment lists plasma membrane. The source concerns HCMV uptake, not a direct EGF-stimulated endosomal-signaling assay. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9611147 |
| GO:0045296 cadherin binding | HDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by... | UNDECIDED | Summary: E-cadherin-proximal labeling does not resolve this source-specific cadherin-binding claim. Reason: The recovered PMID:25468996 Methods and Results use E-cadherin-BirA proximity labeling in human MKN28 cells, followed by streptavidin enrichment and mass spectrometry with negative controls and replicate filtering. Such a signal can include indirect neighbors; it is not a pair-specific binding assay. The EGFR target row in the supplementary dataset and any independent EGFRβcadherin validation were not recovered. Retain the positive curated HDA source as unresolved binding evidence, without claiming absence from cadherin neighborhoods or treating proximity as physical binding. Supporting Evidence: |
| 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 migration in the measured mammary-cell context. Reason: PMID:25678558 uses human MCF10A cells and reports EGF-dependent migration together with EGFR/MEK-inhibitor effects, including changes in speed and directional persistence. EGFR provides an active signaling input to this response; the positive process assertion is retained. The paper separately investigates NAV3-dependent microtubule effects. The result supports a contextual motility role rather than assigning the downstream cytoskeletal machinery to EGFR or claiming that every cell type responds identically. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28479384 Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in ... | KEEP AS NON CORE | Summary: EGFR association with LAPTM4B is retained in the autophagy-regulatory context. Reason: The verified PMID:28479384 abstract explicitly reports that BECN1 competes with EGFR for LAPTM4B binding, which supports the imported positive association. Full operative Methods and construct-resolved results were not recovered. LAPTM4B trafficking and autophagy roles do not establish a more specific catalytic or receptor partner class. Retain generic binding with this access boundary, without borrowing purified-interface or isoform details from other papers. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | IMP PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | MODIFY | Summary: The cellular experiment measures ligand-activated EGFR signaling. Reason: The original EGF-response experiments use human HeLa, MCF-7 and MDA-MB-231 cells and monitor EGFR Tyr1068 phosphorylation alongside downstream Akt. Epidermal growth factor receptor activity is more informative for this intact cellular receptor context than generic tyrosine kinase activity. The separately expressed EGFR His676βAla1210 fragment is used for binding experiments and is not treated as a complete ligand-responsive receptor. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | KEEP AS NON CORE | Summary: EGFR is recovered with the RQCD1/GIGYF/GRB10/Akt interaction system. Reason: The original GST-RQCD1 pull-down recovers EGFR, Akt, GIGYF1/2 and GRB10 from cellular extracts; separate binding experiments test individual partners against RQCD1. These establish physical association, but do not demonstrate a binary EGFR contact with every member of the imported aggregate support set. The partners also span catalytic and noncatalytic classes, so one kinase-binding replacement would misdescribe the whole assertion. The positive generic association is retained under the project-specific policy. Supporting Evidence: |
| 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 initiates the EGF-dependent signaling response examined in the RQCD1 study. Reason: The original experiments measure EGF-dependent EGFR and Akt phosphorylation and show that RQCD1 depletion impairs Akt activation without equivalently suppressing receptor Tyr1068 phosphorylation. This places the measured RQCD1-dependent step downstream of receptor activation while preserving EGFR participation in its own signaling pathway. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | KEEP AS NON CORE | Summary: EGFR is recovered in a signaling-associated protein complex. Reason: The original cellular pull-downs and co-association experiments support an EGFR-containing protein complex involving RQCD1 and associated signaling proteins. The broadly named protein-containing complex is retained for this measured context, without claiming that all recovered proteins form one fixed stoichiometric native assembly or each contacts EGFR directly. Supporting Evidence: |
| 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 promotes downstream Akt serine phosphorylation. Reason: The original EGF experiments measure Akt Ser473 phosphorylation and its dependence on RQCD1. This supports a positive regulatory role of the receptor pathway in serine phosphorylation. The serine residue is on downstream Akt; the result does not demonstrate direct EGFR serine-kinase chemistry. Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | IMP PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | ACCEPT | Summary: The DGK-theta study examines ligand-responsive EGFR activity. Reason: The source abstract measures EGF-induced receptor phosphorylation and uses EGFR and PKC perturbations to distinguish receptor activation from feedback phosphorylation. This is consistent with the receptor activity annotation, without treating the downstream lipid kinase as an EGFR catalytic domain. Exact expression constructs were not recovered from the original Methods. Supporting Evidence: |
| 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 promotes DGK-theta recruitment to the plasma membrane. Reason: The complete abstract explicitly reports DGK-theta translocation from cytosol to plasma membrane after EGF stimulation and states that EGFR and PKC activation are required. EGFR therefore contributes a signaling step to the localization process; it is not merely the transported cargo. The result is retained as a contextual localization-regulatory output. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:22732145 Diacylglycerol kinase ΞΈ counteracts protein kinase C-mediate... | ACCEPT | Summary: EGFR colocalizes with recruited DGK-theta at the plasma membrane. Reason: The source abstract describes plasma-membrane colocalization of DGK-theta and EGFR before internalization into receptor-containing vesicles. This positive compartment observation supports the existing annotation. It does not imply exclusive surface residence, and the full imaging protocol was unavailable. Supporting Evidence: |
| 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 inhibition promotes cardiogenic differentiation of human bone-marrow mesenchymal stem cells. Reason: The complete abstract reports that the EGFR inhibitor compound 56 promotes cardiogenic differentiation of human bone-marrow-derived mesenchymal stem cells; miR-133a targeting EGFR also increases cardiac markers. This direction is consistent with the imported negative-regulation term, whose current definition itself cites this study. Retain the curator-supported IMP in this bounded differentiation context, rather than changing it to migration. Full Methods were inaccessible, so inhibitor selectivity, marker details, EGFR-specific rescue and mature electromechanical integration were not independently established. The evidence does not warrant a claim about all cardiocytes or all differentiation settings. Supporting Evidence: |
| GO:0005768 endosome | IDA PMID:16554368 The ESCRT-III subunit hVps24 is required for degradation but... | ACCEPT | Summary: Internalized EGFR occupies endosomal compartments in the hVps24 study. Reason: The retained original text explicitly reports EGFR accumulation in multivesicular endosomes after hVps24 depletion and separates impaired degradation from signaling silencing. This supports the receptor cargo location. It does not assign ESCRT assembly or membrane-remodeling activity to EGFR. The normal cache omits operative Methods/Results, and the reported microscopy is not represented here as independently inspected figure pixels. Supporting Evidence: |
| GO:0008284 positive regulation of cell population proliferation | IMP PMID:27057632 Tumor-suppressive miR-218-5p inhibits cancer cell proliferat... | ACCEPT | Summary: Direct EGFR depletion reduces proliferation-associated CCK8 readouts in human lung-cancer cells. Reason: The original independently depletes EGFR with two siRNAs in human A549 and H1975 cells, verifies reduced EGFR protein and reports lower CCK8 proliferation indices in Figure 4. This supports the imported positive-regulation annotation as a principal mitogenic output of EGFR signaling; being downstream of receptor activity is not by itself a reason to mark it non-core. CCK8 is a metabolic viability/proliferation proxy, and the source does not separately resolve division from survival. The miRNA xenograft experiments and EGFR transcript-variant 4 3-prime-UTR reporter are different assays, not an EGFR-specific in-vivo rescue or protein-isoform comparison. Remove the inherited MAPK/PI3K wording because those pathways were not directly assayed here. Supporting Evidence: |
| 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: Positive regulation of the ERK cascade is a core EGFR signaling output. Reason: Retain the curated IMP assertion: the source abstract places the miR-221/222 response downstream of EGFR and MEK inhibition, consistent with the established receptorβERK signaling role. This bounded read did not recover the original phospho-ERK experiment or complete pathway dissection, so it does not independently authenticate particular doses, constructs, or every RASβRAF intermediate. The clearly correct biological function is retained with explicit deference to the experimental curation. Supporting Evidence: |
| GO:0030307 positive regulation of cell growth | IDA PMID:15467833 CEACAM1 modulates epidermal growth factor receptor--mediated... | MODIFY | Summary: EGFR promotes the proliferative response to EGF measured in this study. Reason: Current cell growth denotes increasing individual cell size. The operative experiment estimates cell number by MTT, while the liver arm measures PCNA; neither measures individual cell size. EGFR expression increases the EGF response in MCF-7 cells, whereas CEACAM1-4L attenuates it. The human EGFR cDNA is identified in the Acknowledgments. Refine the positive EGFR process to population proliferation without transferring the inhibitory sign of CEACAM1 to EGFR. Proposed replacements: positive regulation of cell population proliferation Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23912460 Hyperactivation of EGFR and downstream effector phospholipas... | MODIFY | Summary: EGFR associates with the kinase-anchoring scaffold FAM83B. Reason: PMID:23912460 reports reciprocal tagged EGFRβFAM83B immunoprecipitation with a GFP control in 293T cells and a separate endogenous association in MDA468 cells. The transfected-cell Methods include formaldehyde fixation before lysis, so this is not a purified binary assay. Independent official FAM83B evidence identifies kinase anchoring and organization of signaling components, supporting the scaffold partner class. The protein is not assigned phospholipase catalysis merely because manipulating it changes PLD activity, and its signaling activities are not transferred to EGFR. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25311788 EGFR phosphorylates and inhibits lung tumor suppressor GPRC5... | MODIFY | Summary: EGFR coassociates with the orphan receptor GPRC5A. Reason: PMID:25311788 directly reports reciprocal EGFR/GPRC5A immunoprecipitation in HEK293T cells, with normal-IgG control and separate EGF/inhibitor phosphorylation experiments. The official GPRC5A record identifies an orphan GPCR and carries a curated GPCR-activity assertion, supporting this partner-class refinement. Lack of an identified ligand does not by itself erase that classification. The association does not show that EGFR is a GPRC5A agonist, that this experiment measures G-protein coupling, or that all natural EGFR products behave equivalently. Proposed replacements: G protein-coupled receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25666625 Epidermal growth factor receptor (EGFR) signaling requires a... | KEEP AS NON CORE | Summary: EGFR forms an AGR2-associated folding-intermediate complex. Reason: The recovered PMID:25666625 experiments use thiol trapping and reducing versus nonreducing immunoprecipitation to identify an AGR2βEGFR mixed-disulfide complex in human cells; A431 experiments and mass spectrometry provide additional support. This establishes the positive association. A thioredoxin-family fold and a mixed-disulfide intermediate alone do not establish a complete catalytic isomerase cycle for the partner, so enzyme-binding specificity is not forced. Retain the interaction with its folding and assay context, without transferring AGR2 function to EGFR. Supporting Evidence: |
| GO:0009986 cell surface | IDA PMID:25666625 Epidermal growth factor receptor (EGFR) signaling requires a... | ACCEPT | Summary: Human EGFR is detected at the cell surface in the AGR2 study. Reason: PMID:25666625 directly measures EGFR on nonpermeabilized H460 and A431 cells with antibody 528, flow cytometry and surface biotinylation. AGR2 perturbation changes surface distribution while the study separately assesses EGFR transcript and total protein. These are positive surface-localization measurements that support the existing annotation; they do not make every truncated natural product a membrane receptor. Supporting Evidence: |
| GO:0031901 early endosome membrane | IDA PMID:17714434 Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth... | ACCEPT | Summary: Internalized endogenous EGFR occupies early-endosome membranes. Reason: The original Results and Figure 6 describe endogenous EGFR on the limiting membrane of early-appearing endosomes in Vps22-depleted HEp-2 cells; EEA1 colocalization independently supports early-endosome retention. Cryosection labeling reproduced the result without antibody prebinding. This directly supports the membrane location. The location itself should not be used to claim prolonged signaling: Vps22 depletion did not prolong ERK activation in the same study. Supporting Evidence: |
| GO:0097489 multivesicular body, internal vesicle lumen | IDA PMID:17714434 Vps22/EAP30 in ESCRT-II mediates endosomal sorting of growth... | MODIFY | Summary: The observed EGFR pool is associated with the membrane of internal vesicles in multivesicular bodies. Reason: Figure 6 and the original Results place endogenous EGFR on intraluminal vesicles; Figure 7 independently demonstrates protease-protected sequestration into those vesicles. The membrane term describes this receptor-associated pool more precisely than the enclosed aqueous-volume term. Preserve the positive experimental sorting evidence. Protease protection is not evidence of a freely soluble luminal EGFR pool, and the refinement does not deny that the cytoplasmic domain becomes enclosed when the vesicle buds inward. Proposed replacements: multivesicular body, internal vesicle membrane Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:8305738 The human GRB2 and Drosophila Drk genes can functionally rep... | MODIFY | Summary: Activated human EGFR binds the SH2-dependent interface of worm Sem-5. Reason: The authentic PMID:8305738 original Figure 2 and Figure 5 captions describe GST- or TrpE-Sem-5 binding to activated human EGFR from cell lysates, with fusion-protein controls and mutations in the Sem-5 SH2 domain. The mutations abolish the measured association, supporting an SH2-interface refinement. This is an explicitly cross-species experiment using C. elegans Sem-5, not a native human complex. Worm rescue and human-receptor binding are separate observations; no exact natural EGFR insert sequence or purified two-protein assay is claimed. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:23418353 The E3 ubiquitin ligases RNF126 and Rabring7 regulate endoso... | ACCEPT | Summary: EGFR associates with the E3 ubiquitin ligase RNF126. Reason: The verified PMID:23418353 abstract explicitly reports RNF126 association with EGFR and E3 activity with defined E2 enzymes, with ubiquitin-binding-domain and cellular sorting context. The imported Q91YL2 identifier is the mouse RNF126 protein and is preserved; independent official evidence supports that ligase identity. The original full Methods were unavailable, so the association is not relabeled as a purified human-human experiment or assigned an unverified construct sequence. Retain the correct partner-class binding assertion without assigning ligase catalysis to EGFR. Supporting Evidence: |
| GO:0010008 endosome membrane | IDA PMID:22719997 SNX12 role in endosome membrane transport. | ACCEPT | Summary: Internalized EGFR is observed on the limiting membrane of endosomes in human HeLa cells. Reason: The original EGF-uptake experiments identify endogenous EGFR by immunofluorescence in HeLa cells. Figure 4CβG specifically places EGFR on the limiting membrane of enlarged Rab5Q79L endosomes after Hrs or SNX3 depletion; SNX12 restores sorting toward the lumen. Thus the source supports endosome membrane, rather than only a broad endomembrane compartment. The manipulated proteins are trafficking factors, not an EGFR transgene. This evidence establishes localization; the inherited statement that EGFR continues to signal at this location is not measured here and should be omitted. Supporting Evidence: |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | KEEP AS NON CORE | Summary: EGFR is reproducibly detected in isolated focal-adhesion fractions from human HFF1 cells. Reason: The publisher workbook identifies EGFR in the reproducible focal-adhesion fraction: Table 7 lists control spectral counts 4, 7, 10 and blebbistatin counts 7, 3, 4; Table 9 peptide groups independently reproduce these totals. The authors use detection in at least two of three runs, and EGFR is present in all six. The fractionation may retain membrane, cytoskeletal and cytosolic material, and the study explicitly allows contaminants; this does not demonstrate a target-specific error in the positive HDA. Retain the measured association as non-core. EGFR is absent from the target lists for the orthogonal validation Tables 5/6; no EGFR-specific migration assay or microscopy is established here. The historical IPI isoform label is a database assignment, not proof of isoform-discriminating peptides. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9852145 Interaction of ZPR1 with translation elongation factor-1alph... | KEEP AS NON CORE | Summary: Human EGFR associates with recombinant mouse ZPR1. Reason: PMID:9852145 Results and Fig. 3A explicitly recover the 180-kDa EGFR from human A431 lysate with immobilized mouse ZPR1, matching the imported Q62384 partner. The purified two-protein experiment in Fig. 3D instead concerns yeast ZPR1 and eEF1A and must not be transferred to EGFR. ZPR1 zinc fingers do not establish a transcription-factor class. Retain the positive generic association as non-core under the ClinGen project instruction; no supported narrower binding class is established here. Supporting Evidence: |
| GO:0043235 receptor complex | IDA PMID:23382219 Structural basis for endosomal trafficking of diverse transm... | UNDECIDED | Summary: The exact receptor-complex assertion could not be verified from the recovered source material. Reason: The current term is signaling receptor complex. The normal cache contains the abstract and Discussion but omits the operative Results and SI Methods. Additional indexed original passages concern PX-FERM cargo motifs and a P-selectin structure; the target-resolved EGFR complex experiment was not recovered. These passages do not verify the inherited claim about all EGFR homo- and ERBB heterodimers. Retain the source assertion unresolved rather than call it wrong or infer a complex composition from unrelated cargo results. Supporting Evidence: |
| GO:0007611 learning or memory | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Learning and memory is supported as a rodent physiological context, with a donor-species caveat. Reason: The current G3V6K6 donor is rat and carries GO:0007611 IDA to PMID:20639532. The actual original distinguishes rat hippocampal-neuron experiments from C57BL/6J mouse Morris-water-maze experiments. EGF/gefitinib infusion affects learning and probe-trial retention, with swimming/vision controls; the EGF acquisition trend is not uniformly significant. Thus the original contains genuine behavioral evidence, but it does not directly test rat or human memory, nor a gene-specific genetic rescue. Retain this broader contextual transfer as non-core and explicitly preserve the rat-record versus mouse-assay mismatch rather than changing the source identity or calling the whole biological role false. |
| GO:0071364 cellular response to epidermal growth factor stimulus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Rat neurons provide an explicit cellular EGF-response assay. Reason: PMID:20639532 uses rat hippocampal neurons, EGF stimulation and EGFR-Y1068, STAT5 and AKT phosphorylation readouts, including the altered kinetics after CPEB3 knockdown. This supports the exact donor response claim, distinct from the mouse behavioral arm. Keep the broad response context non-core alongside the more specific EGFR receptor/pathway assertions; do not suggest that the receptor is merely a passive EGF substrate. |
| GO:0001934 positive regulation of protein phosphorylation | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: EGFR contributes to E2-induced phosphorylation responses in breast cancer-associated fibroblasts. Reason: The original human fibroblast experiments show E2/G1-dependent ERK phosphorylation requiring both EGFR and GPR30/GPER1, with shRNA and pathway-inhibitor controls. This supports positive regulation of phosphorylation in that signaling context, without assigning estradiol receptor activity or all downstream kinase reactions to EGFR. Supporting Evidence: |
| GO:0003682 chromatin binding | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: A nuclear EGFR-containing complex associates with the CCND1 promoter. Reason: The original ChIP experiments recover the CCND1 promoter with EGFR antibodies after E2 stimulation, and the response depends on GPR30/GPER1. Reciprocal nuclear co-immunoprecipitation and promoter-reporter experiments support this chromatin-associated context. ChIP establishes association with chromatin; it does not demonstrate purified EGFR recognition of a particular DNA sequence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | MODIFY | Summary: EGFR associates with the G protein-coupled receptor GPER1. Reason: The original nuclear-fraction experiments in human cancer-associated fibroblasts use reciprocal co-immunoprecipitation of GPR30/GPER1 and phosphorylated EGFR, rather than inference solely from shared ERK responses. The exact imported partner Q99527 is the officially classified G protein-coupled receptor GPER1. GPCR binding therefore captures the partner class without claiming a purified interface, universal nuclear residence, or EGFR-mediated estrogen binding. Proposed replacements: G protein-coupled receptor binding Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: The experiment detects nuclear EGFR in human breast cancer-associated fibroblasts. Reason: The original nuclear fractionation, reciprocal co-immunoprecipitation and phospho-EGFR immunostaining with DAPI and preimmune-serum controls support a nuclear pool after E2 stimulation. This source-specific pool is retained as contextual; the assay does not imply that all EGFR or all natural products reside in the nucleus. Supporting Evidence: |
| 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 contributes to transcriptional activation in the GPER1-dependent fibroblast response. Reason: The original study measures E2-dependent CCND1 promoter activity and target transcript induction, with EGFR/GPER1 knockdown and mutations of the promoter response elements. These experiments support a positive transcriptional contribution. They do not establish EGFR as a sequence-specific DNA-binding transcription factor. Supporting Evidence: |
| 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 ERK activation in the E2/GPER1 fibroblast signaling context. Reason: The original phospho-ERK readout depends on EGFR and GPER1 and is inhibited by pathway perturbation. This is active signaling participation, not an inference from expression alone. It supports the same principal ERK-cascade output accepted in other EGFR rows, while retaining this fibroblast and E2/GPER1 context. Acceptance does not assign MAP3K catalysis to EGFR or require a separate core unit. Supporting Evidence: |
| GO:0071392 cellular response to estradiol stimulus | IDA PMID:20551055 Nuclear alternate estrogen receptor GPR30 mediates 17beta-es... | KEEP AS NON CORE | Summary: EGFR participates in the measured cellular response to estradiol. Reason: In primary human cancer-associated fibroblasts, EGFR knockdown or inhibition disrupts E2-induced phosphorylation and transcriptional responses involving GPER1. This supports participation in the response under the tested conditions. It does not establish direct estradiol binding to EGFR or generalize the result to every cell type. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1247999 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1247999 (EGFRvIII mutant binds chaperone proteins HSP90 and CDC37), the captured typed path 1247999 --input--> 1214162 reaches human EGFR entity 1214162 (EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1247999 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1248002 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1248002 (Ligand-independent dimerization of EGFRvIII mutant), the captured typed path 1248002 --input--> 1248004; 1248004 --hasComponent--> 1214162 reaches human EGFR entity 1214162 (EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1248002 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1248655 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1248655 (Trans-autophosphorylation of EGFRvIII mutant dimers), the captured typed path 1248655 --input--> 1248010; 1248010 --hasComponent--> 1248004; 1248004 --hasComponent--> 1214162 reaches human EGFR entity 1214162 (EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1248655 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637764 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637764 (Binding of GRB2:GAB1 complex to p-EGFRvIII mutant), the captured typed path 5637764 --input--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637764 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637765 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637765 (Binding of PI3K to complex of GRB2:GAB1 and p-EGFRvIII), the captured typed path 5637765 --input--> 5637694; 5637694 --hasComponent--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637765 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637766 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637766 (Binding of SHC1 to p-5Y-EGFRvIII), the captured typed path 5637766 --input--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637766 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637770 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637770 (Binding of GRB2:SOS1 complex to phosphorylated EGFRvIII), the captured typed path 5637770 --input--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637770 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637792 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637792 (PLC-gamma 1 binds to p-EGFRvIII mutant), the captured typed path 5637792 --input--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637792 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637794 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637794 (EGFRvIII does not bind CBL), the captured typed path 5637794 --input--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. The FailedReaction describes deficient mutant binding or ubiquitination, not absence of the membrane-localized receptor. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637794 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637795 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637795 (Phosphorylation of PLC-gamma 1 by p-EGFRvIII mutant), the captured typed path 5637795 --input--> 5637698; 5637698 --hasComponent--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637795 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637796 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637796 (Phosphorylation of SHC1 by p-5Y-EGFRvIII), the captured typed path 5637796 --input--> 5637701; 5637701 --hasComponent--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637796 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637798 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637798 (Phosphorylated SHC1 in complex with p-5Y-EGFRvIII recruits GRB2:SOS1 complex), the captured typed path 5637798 --input--> 5637703; 5637703 --hasComponent--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637798 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637800 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637800 (Dissociation of phosphorylated PLC-gamma 1 from p-EGFRvIII mutant), the captured typed path 5637800 --output--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637800 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637801 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637801 (Conversion of PIP2 to PIP3 by PI3K bound to phosphorylated EGFRvIII), the captured typed path 5637801 --catalystActivity--> 9037678; 9037678 --physicalEntity--> 5637693; 5637693 --hasComponent--> 5637694; 5637694 --hasComponent--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637801 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637806 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637806 (SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with p-EGFRvIII)), the captured typed path 5637806 --catalystActivity--> 5637803; 5637803 --physicalEntity--> 5637697; 5637697 --hasComponent--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637806 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5637808 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5637808 (SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and p-EGFRvIII)), the captured typed path 5637808 --catalystActivity--> 5637804; 5637804 --physicalEntity--> 5637704; 5637704 --hasComponent--> 5637703; 5637703 --hasComponent--> 1248654; 1248654 --hasComponent--> 1248651; 1248651 --hasComponent--> 1248649 reaches human EGFR entity 1248649 (p-5Y-EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5637808 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5638137 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5638137 (EGFRvIII cancer variant does not bind EGF ligand), the captured typed path 5638137 --input--> 1248004; 1248004 --hasComponent--> 1214162 reaches human EGFR entity 1214162 (EGFRvIII [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The recovered target witnesses in this event are disease variants; their shared membrane location is retained without generalizing mutant ligand behavior or equating a deletion mutant with a natural isoform. The FailedReaction describes deficient mutant binding or ubiquitination, not absence of the membrane-localized receptor. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5638137 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1250195 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1250195 (SHC1 phosphorylation by ERBB2 heterodimers), the captured typed path 1250195 --input--> 1248746; 1248746 --hasComponent--> 1963588; 1963588 --hasMember--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1250195 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306957 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1306957 (PIP2 to PIP3 conversion by PI3K bound to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR), the captured typed path 1306957 --catalystActivity--> 1306960; 1306960 --physicalEntity--> 1306961; 1306961 --hasComponent--> 1306962; 1306962 --hasComponent--> 1306958; 1306958 --hasComponent--> 1963587; 1963587 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1306957 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306963 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1306963 (Binding of GRB2:GAB1 to p-ERBB2:p-EGFR), the captured typed path 1306963 --input--> 1963587; 1963587 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1306963 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1306965 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1306965 (Binding of PI3K to GRB2:GAB1 in complex with phosphorylated heterodimer of ERBB2 and EGFR), the captured typed path 1306965 --input--> 1306958; 1306958 --hasComponent--> 1963587; 1963587 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1306965 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177923 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177923 (Sustained activation of SRC kinase by SHP2), the captured typed path 177923 --catalystActivity--> 180501; 180501 --physicalEntity--> 180269; 180269 --hasComponent--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177923 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177924 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177924 (Dephosphorylation of Gab1 by SHP2), the captured typed path 177924 --output--> 180503; 180503 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177924 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177925 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177925 (SHC1 binds to the phosphorylated EGF receptor:ligand complex), the captured typed path 177925 --input--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177925 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177926 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177926 (Dephosphorylation of PAG by SHP2), the captured typed path 177926 --catalystActivity--> 180501; 180501 --physicalEntity--> 180269; 180269 --hasComponent--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177926 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177927 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177927 (PI3K binds to EGF:EGFR:GRB2:GAB1), the captured typed path 177927 --input--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177927 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177930 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177930 (GAB1 phosphorylation by EGFR kinase), the captured typed path 177930 --catalystActivity--> 180302; 180302 --activeUnit--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177930 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177933 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177933 (SHC1 phosphorylation by phosphorylated EGFR), the captured typed path 177933 --catalystActivity--> 9624433; 9624433 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177933 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177934 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177934 (EGFR autophosphorylation), the captured typed path 177934 --output--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177934 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177936 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177936 (GRB2:SOS1 binds to phosphorylated SHC1 in complex with EGFR), the captured typed path 177936 --input--> 180337; 180337 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177936 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177937 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177937 (Phosphorylation of EGFR by SRC kinase), the captured typed path 177937 --output--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177937 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177938 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177938 (SOS1-mediated nucleotide exchange of RAS (EGF:EGFR:GRB2:SOS1)), the captured typed path 177938 --catalystActivity--> 177932; 177932 --physicalEntity--> 179820; 179820 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177938 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177939 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177939 (PI3K converts phosphatidylinositol-4,5-bisphosphate (PIP2) to phosphatidylinositol-3,4,5-trisphosphate (PIP3)), the captured typed path 177939 --catalystActivity--> 179881; 179881 --physicalEntity--> 179791; 179791 --hasComponent--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177939 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177941 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177941 (GRB2:GAB1 binds to phosphorylated EGFR), the captured typed path 177941 --input--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177941 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177943 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177943 (GRB2:SOS1 complex binds to EGF:EGFR complex), the captured typed path 177943 --input--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177943 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177944 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177944 (Activation of SHP2 through the binding to phospho-Gab1), the captured typed path 177944 --input--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177944 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177945 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177945 (SOS1-mediated nucleotide exchange of RAS (EGF:EGFR:SHC1:GRB2:SOS1)), the captured typed path 177945 --catalystActivity--> 180290; 180290 --physicalEntity--> 180331; 180331 --hasComponent--> 180337; 180337 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177945 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182969 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-182969 (Phosphorylation of CBL (EGFR:CBL)), the captured typed path 182969 --output--> 182953; 182953 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-182969 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182986 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-182986 (CBL-mediated ubiquitination of CIN85), the captured typed path 182986 --output--> 182936; 182936 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-182986 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182990 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-182990 (Sprouty sequesters CBL away from active EGFR), the captured typed path 182990 --input--> 182961; 182961 --hasComponent--> 182953; 182953 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-182990 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182993 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-182993 (Ubiquitination of stimulated EGFR (CBL)), the captured typed path 182993 --input--> 182953; 182953 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-182993 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-182994 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-182994 (Assembly of EGFR complex in clathrin-coated vesicles), the captured typed path 182994 --input--> 182948; 182948 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-182994 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183002 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183002 (Beta-Pix:CDC42:GTP binds CBL in EGF:p-6Y-EGFR:CBL:CIN85), the captured typed path 183002 --input--> 182946; 182946 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183002 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183036 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183036 (Ubiquitination of stimulated EGFR (CBL:GRB2)), the captured typed path 183036 --input--> 182948; 182948 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183036 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183051 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183051 (CBL ubiquitinates Sprouty), the captured typed path 183051 --input--> 182935; 182935 --hasComponent--> 182960; 182960 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183051 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183055 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183055 (Binding of CBL to EGFR), the captured typed path 183055 --input--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183055 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183058 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183058 (Phosphorylation of CBL (EGFR:GRB2:CBL)), the captured typed path 183058 --output--> 182948; 182948 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183058 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183067 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183067 (Localization of CBL:GRB2 to the membrane), the captured typed path 183067 --input--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183067 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183072 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183072 (EGFR non-clathrin mediated endocytosis), the captured typed path 183072 --input--> 182953; 182953 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183072 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183084 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183084 (CBL escapes CDC42-mediated inhibition by down-regulating the adaptor molecule Beta-Pix), the captured typed path 183084 --input--> 182932; 182932 --hasComponent--> 182948; 182948 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183084 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-183089 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-183089 (CBL binds and ubiquitinates phosphorylated Sprouty), the captured typed path 183089 --input--> 182953; 182953 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-183089 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963563 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1963563 (MATK (CSK homologous kinase) binds phosphorylated ERBB2), the captured typed path 1963563 --input--> 1963588; 1963588 --hasMember--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1963563 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963581 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1963581 (Trans-autophosphorylation of p-Y877-ERBB2 heterodimers), the captured typed path 1963581 --output--> 1963580; 1963580 --hasMember--> 1248703; 1248703 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1963581 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963582 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1963582 (Trans-autophosphorylation of ERBB2 heterodimers), the captured typed path 1963582 --output--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1963582 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212706 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-212706 (Phospholipase C-gamma1 binds to the activated EGF receptor), the captured typed path 212706 --input--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-212706 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212710 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-212710 (EGFR activates PLC-gamma1 by phosphorylation), the captured typed path 212710 --catalystActivity--> 212705; 212705 --activeUnit--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-212710 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-212713 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-212713 (Active PLC-gamma1 dissociates from EGFR), the captured typed path 212713 --output--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-212713 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2179387 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-2179387 (Mature HBEGF binds to EGFR, triggering dimerisation and autophosphorylation of the receptor), the captured typed path 2179387 --input--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-2179387 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2179407 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-2179407 (SOS1-mediated nucleotide exchange of RAS (HB-EFG-initiated)), the captured typed path 2179407 --catalystActivity--> 2179400; 2179400 --physicalEntity--> 2179409; 2179409 --hasComponent--> 2179410; 2179410 --hasComponent--> 2179388; 2179388 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-2179407 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2179415 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-2179415 (GRB2:SOS1 binds to HBEGF:p-Y-EGFR), the captured typed path 2179415 --input--> 2179410; 2179410 --hasComponent--> 2179388; 2179388 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-2179415 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-2316434 (PI3K phosphorylates PIP2 to PIP3), the captured typed path 2316434 --catalystActivity--> 2316433; 2316433 --physicalEntity--> 2316432; 2316432 --hasMember--> 179791; 179791 --hasComponent--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-2316434 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-2400009 (PI3K inhibitors block PI3K catalytic activity), the captured typed path 2400009 --input--> 2400011; 2400011 --hasMember--> 2316432; 2316432 --hasMember--> 179791; 179791 --hasComponent--> 180286; 180286 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-2400009 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672965 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-5672965 (RAS GEFs promote RAS nucleotide exchange), the captured typed path 5672965 --catalystActivity--> 5672963; 5672963 --physicalEntity--> 5672601; 5672601 --hasMember--> 179820; 179820 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-5672965 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6785636 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-6785636 (Phosphorylated ERBB2 heterodimers bind MEMO1), the captured typed path 6785636 --input--> 1963588; 1963588 --hasMember--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-6785636 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-6785648 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-6785648 (MEMO1 binds RHOA:GTP:DIAPH1), the captured typed path 6785648 --input--> 6785640; 6785640 --hasComponent--> 1963588; 1963588 --hasMember--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-6785648 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8847995 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8847995 (Activated ERBB2 binds PTK6 (BRK)), the captured typed path 8847995 --input--> 1963588; 1963588 --hasMember--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8847995 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8848005 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8848005 (ERBB2 promotes PTK6 autophosphorylation), the captured typed path 8848005 --output--> 1963588; 1963588 --hasMember--> 1963585; 1963585 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8848005 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864105 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8864105 (PTPN18 binds ERBB2:EGFR heterodimers), the captured typed path 8864105 --input--> 1963587; 1963587 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8864105 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8864125 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8864125 (PTPN18 dephosphorylates ERBB2 at Y1196, Y1112 and Y1248), the captured typed path 8864125 --input--> 8864106; 8864106 --hasComponent--> 1963587; 1963587 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8864125 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8866279 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8866279 (Epsin family proteins bind ubiquitinated cargo), the captured typed path 8866279 --input--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8866279 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867041 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8867041 (EGFR phosphorylates EPS15), the captured typed path 8867041 --catalystActivity--> 8867039; 8867039 --activeUnit--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8867041 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867044 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8867044 (EGFR binds EPS15, EPN1, EPS15L1), the captured typed path 8867044 --input--> 182946; 182946 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8867044 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867047 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8867047 (PTPN3 dephosphorylates EPS15), the captured typed path 8867047 --input--> 8867035; 8867035 --hasComponent--> 182946; 182946 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8867047 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867754 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8867754 (F- and N- BAR domain proteins bind the clathrin-coated pit), the captured typed path 8867754 --input--> 8868051; 8868051 --hasComponent--> 8867753; 8867753 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8867754 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8867756 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8867756 (CLASP proteins and cargo are recruited to the nascent clathrin-coated pit), the captured typed path 8867756 --input--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8867756 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868071 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868071 (Clathrin recruits PIK3C2A), the captured typed path 8868071 --input--> 8867753; 8867753 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868071 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868072 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868072 (Clathrin-associated PIK3C2A phosphorylates PI(4)P to PI(3,4)P2), the captured typed path 8868072 --catalystActivity--> 8868073; 8868073 --physicalEntity--> 8868051; 8868051 --hasComponent--> 8867753; 8867753 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868072 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868230 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868230 (SNX9 recruits components of the actin polymerizing machinery), the captured typed path 8868230 --input--> 8867751; 8867751 --hasComponent--> 8868632; 8868632 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868230 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868236 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868236 (BAR domain proteins recruit dynamin), the captured typed path 8868236 --input--> 8868232; 8868232 --hasComponent--> 8867751; 8867751 --hasComponent--> 8868632; 8868632 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868236 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868648 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868648 (SYNJ hydrolyze PI(4,5)P2 to PI(4)P), the captured typed path 8868648 --output--> 8868629; 8868629 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868648 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868651 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868651 (Endophilins recruit synaptojanins to the clathrin-coated pit), the captured typed path 8868651 --input--> 8868234; 8868234 --hasComponent--> 8868232; 8868232 --hasComponent--> 8867751; 8867751 --hasComponent--> 8868632; 8868632 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868651 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8868661 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8868661 (Dynamin-mediated GTP hydrolysis promotes vesicle scission), the captured typed path 8868661 --input--> 8868629; 8868629 --hasComponent--> 8867603; 8867603 --hasMember--> 8866261; 8866261 --hasComponent--> 8866252; 8866252 --hasMember--> 8867037; 8867037 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8868661 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8951490 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8951490 (CIN85 dissociates from EGF:p-6Y-EGFR:CBL:Beta-Pix:CDC42:GTP:CIN85), the captured typed path 8951490 --input--> 8951489; 8951489 --hasComponent--> 182946; 182946 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8951490 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9018572 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9018572 (EGFR phosphorylates NOTCH3), the captured typed path 9018572 --output--> 179882; 179882 --hasComponent--> 179860; 179860 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9018572 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9018573 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9018573 (NOTCH3 binds activated EGFR), the captured typed path 9018573 --input--> 179882; 179882 --hasComponent--> 179860; 179860 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9018573 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9625482 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9625482 (PTK2 binds activated EGFR), the captured typed path 9625482 --input--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9625482 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9625487 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9625487 (PTK2 autophosphorylates downstream of EGFR), the captured typed path 9625487 --input--> 9625453; 9625453 --hasComponent--> 9624425; 9624425 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9625487 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664588 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664588 (ERBB2 KD mutants trans-autophosphorylate), the captured typed path 9664588 --output--> 9664606; 9664606 --hasMember--> 9664609; 9664609 --hasComponent--> 9664598; 9664598 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664588 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664918 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664918 (Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:GAB1), the captured typed path 9664918 --input--> 9664917; 9664917 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664918 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664933 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664933 (Phosphorylated heterodimers of ERBB2 KD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K), the captured typed path 9664933 --input--> 9664921; 9664921 --hasComponent--> 9664917; 9664917 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664933 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664940 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664940 (PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR converts PIP2 to PIP3), the captured typed path 9664940 --catalystActivity--> 9664939; 9664939 --physicalEntity--> 9664932; 9664932 --hasComponent--> 9664921; 9664921 --hasComponent--> 9664917; 9664917 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664940 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664950 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664950 (Phosphorylated heterodimers of ERBB2 KD mutants bind SHC1), the captured typed path 9664950 --input--> 9664606; 9664606 --hasMember--> 9664609; 9664609 --hasComponent--> 9664598; 9664598 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664950 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664976 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664976 (Phosphorylated heterodimers of ERBB2 KD mutants phosphorylate SHC1), the captured typed path 9664976 --input--> 9664947; 9664947 --hasComponent--> 9664606; 9664606 --hasMember--> 9664609; 9664609 --hasComponent--> 9664598; 9664598 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664976 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664983 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664983 (Phosphorylated heterodimers of ERBB2 KD mutants recruit GRB2:SOS1 through SHC1), the captured typed path 9664983 --input--> 9664975; 9664975 --hasComponent--> 9664606; 9664606 --hasMember--> 9664609; 9664609 --hasComponent--> 9664598; 9664598 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664983 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664991 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664991 (RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants), the captured typed path 9664991 --catalystActivity--> 9664990; 9664990 --physicalEntity--> 9664981; 9664981 --hasComponent--> 9664975; 9664975 --hasComponent--> 9664606; 9664606 --hasMember--> 9664609; 9664609 --hasComponent--> 9664598; 9664598 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664991 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665000 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665000 (Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:SOS1), the captured typed path 9665000 --input--> 9665001; 9665001 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665000 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665009 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665009 (RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR), the captured typed path 9665009 --catalystActivity--> 9665008; 9665008 --physicalEntity--> 9664996; 9664996 --hasComponent--> 9665001; 9665001 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665009 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665032 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665032 (Phosphorylated heterodimers of ERBB2 KD mutants and EGFR phosphorylate PLCG1), the captured typed path 9665032 --output--> 9665037; 9665037 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665032 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665034 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665034 (Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind PLCG1), the captured typed path 9665034 --input--> 9665037; 9665037 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665034 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665389 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665389 (Heterodimers of ERBB2 ECD mutants and EGFR trans-autophosphorylate), the captured typed path 9665389 --output--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665389 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665404 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665404 (RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1), the captured typed path 9665404 --catalystActivity--> 9665433; 9665433 --physicalEntity--> 9665437; 9665437 --hasComponent--> 9665441; 9665441 --hasComponent--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665404 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665406 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665406 (Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate SHC1), the captured typed path 9665406 --input--> 9665436; 9665436 --hasComponent--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665406 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665407 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665407 (PI3K bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR converts PIP2 to PIP3), the captured typed path 9665407 --catalystActivity--> 9665463; 9665463 --physicalEntity--> 9665453; 9665453 --hasComponent--> 9665446; 9665446 --hasComponent--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665407 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665408 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665408 (RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR through GRB2), the captured typed path 9665408 --catalystActivity--> 9665452; 9665452 --physicalEntity--> 9665449; 9665449 --hasComponent--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665408 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665409 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665409 (GRB2:SOS1 binds to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR), the captured typed path 9665409 --input--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665409 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665410 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665410 (Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind PLCG1), the captured typed path 9665410 --input--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665410 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665411 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665411 (Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate PLCG1), the captured typed path 9665411 --output--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665411 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665413 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665413 (Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR recruit GRB2:SOS1 through SHC1 ), the captured typed path 9665413 --input--> 9665441; 9665441 --hasComponent--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665413 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665415 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665415 (Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K), the captured typed path 9665415 --input--> 9665446; 9665446 --hasComponent--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665415 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665416 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665416 (Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind SHC1), the captured typed path 9665416 --input--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665416 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665417 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665417 (Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind GRB2:GAB1), the captured typed path 9665417 --input--> 9665380; 9665380 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665417 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665698 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665698 (Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind GRB2:SOS1), the captured typed path 9665698 --input--> 9665917; 9665917 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665698 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665699 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665699 (Phosphorylated heterodimers of ERBB2 TMD/JMD mutants recruit GRB2:SOS1 through SHC1), the captured typed path 9665699 --input--> 9665882; 9665882 --hasComponent--> 9665910; 9665910 --hasComponent--> 9664613; 9664613 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665699 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665700 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665700 (RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants), the captured typed path 9665700 --catalystActivity--> 9665880; 9665880 --physicalEntity--> 9665869; 9665869 --hasComponent--> 9665882; 9665882 --hasComponent--> 9665910; 9665910 --hasComponent--> 9664613; 9664613 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665700 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665701 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665701 (Phosphorylated ERBB2 TMD/JMD heterodimers bind SHC1), the captured typed path 9665701 --input--> 9665910; 9665910 --hasComponent--> 9664613; 9664613 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665701 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665704 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665704 (Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1), the captured typed path 9665704 --output--> 9665925; 9665925 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665704 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665705 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665705 (Phosphorylated heterodimers of ERBB2 TMD/JMD mutants phosphorylate SHC1), the captured typed path 9665705 --input--> 9665887; 9665887 --hasComponent--> 9665910; 9665910 --hasComponent--> 9664613; 9664613 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665705 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665706 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665706 (Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind PLCG1), the captured typed path 9665706 --input--> 9665925; 9665925 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665706 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665707 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665707 (RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR), the captured typed path 9665707 --catalystActivity--> 9665915; 9665915 --physicalEntity--> 9665916; 9665916 --hasComponent--> 9665917; 9665917 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665707 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665709 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665709 (ERBB2 TMD/JMD heterodimers trans-autophosphorylate), the captured typed path 9665709 --output--> 9665877; 9665877 --hasComponent--> 9664613; 9664613 --hasMember--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665709 |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1248744 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-NUL-1248744 (Shc1 binds phosphorylated ERBB2:EGFR heterodimers), the captured typed path 1248744 --input--> 1963587; 1963587 --hasMember--> 1963593; 1963593 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The source is explicitly a chimeric human/mouse model, with human EGFR and mouse signaling components; its R-NUL identifier does not make the EGFR entity mouse-only. CandidateSet 1963587 supplies distinct hasMember and hasCandidate paths, both preserved in the evidence projection; membership is not relabeled as a purified binding experiment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-NUL-1248744 |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1251923 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-NUL-1251923 (Plcg1 binds P-ERBB2:P-EGFR), the captured typed path 1251923 --input--> 1248703; 1248703 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The source is explicitly a chimeric human/mouse model, with human EGFR and mouse signaling components; its R-NUL identifier does not make the EGFR entity mouse-only. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-NUL-1251923 |
| GO:0005886 plasma membrane | TAS Reactome:R-NUL-1251929 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-NUL-1251929 (Plcg1 phosphorylation by P-ERBB2:P-EGFR), the captured typed path 1251929 --input--> 1251930; 1251930 --hasComponent--> 1248703; 1248703 --hasComponent--> 1248702; 1248702 --hasComponent--> 179803 reaches human EGFR entity 179803 (p-6Y-EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The source is explicitly a chimeric human/mouse model, with human EGFR and mouse signaling components; its R-NUL identifier does not make the EGFR entity mouse-only. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-NUL-1251929 |
| GO:0005515 protein binding | IPI PMID:19509291 GAREM, a novel adaptor protein for growth factor receptor-bo... | KEEP AS NON CORE | Summary: Endogenous GAREM1 occurs in an activated EGFR complex. Reason: PMID:19509291 Fig. 1B and Results show endogenous GAREM and GRB2 co-immunoprecipitation with EGFR in EGF-stimulated HeLa cells. The deletion experiments support a GRB2-mediated association; they do not establish an EGFRβGAREM binary interface. GAREM1 is an independently established signaling adaptor, but its adaptor activity should not be transferred to EGFR. Retain this positive association as non-core under the project instruction. The full-length human construct and the shorter GAREM variant are not functionally interchangeable. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18602463 Ataxin-2 associates with the endocytosis complex and affects... | UNDECIDED | Summary: The source-specific EGFRβATXN2 pair remains incompletely adjudicated. Reason: The authentic PMID:18602463 abstract establishes ATXN2 interactions with endophilins and other endocytic proteins and an effect on EGFR trafficking. UniProt Q99700 also curates an EGFR association from this paper, so a positive interaction is plausible and must not be rejected. However, the operative EGFR pair experiment, tested species and construct were not recovered in the bounded access attempts. The foreground endophilin assays do not resolve that pair. Leave this source row undecided pending those details; no wrong-gene or false-interaction claim is made. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10026169 Identification of Grb4/Nckbeta, a src homology 2 and 3 domai... | UNDECIDED | Summary: Human NCK2 SH2 binding is measured against mouse-cell receptor material. Reason: PMID:10026169 Methods specify human NCK2/Grb4 SH2 residues 278β388, but the receptor pull-down uses SV40-immortalized mouse embryonic fibroblast lysate. Fig. 3C reports positive phosphotyrosine-protein recovery. A human EGFR construct was not established. The source-specific human-target mapping remains unresolved, so retain UNDECIDED rather than asserting a direct human EGFR assay. SH2 domain binding is the appropriate conditional refinement if that mapping is resolved; the positive cross-species result is preserved. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15590694 Suppressors of cytokine signaling 4 and 5 regulate epidermal... | KEEP AS NON CORE | Summary: SOCS5 association with EGFR is positively reported. Reason: The authentic PMID:15590694 abstract explicitly reports SOCS5 association with EGFR and receptor downregulation; UniProt O75159 independently preserves the same source-linked association. Retain the biologically supported generic interaction as non-core under the project instruction despite unavailable operative Methods. SH2/SOCS-box dependence of degradation does not by itself map the receptor-binding interface. SOCS5 is a proposed substrate-recognition component of an E3 complex, so this evidence does not establish EGFR binding to an independently catalytic SOCS5 enzyme or warrant transferring ubiquitin-ligase activity to EGFR. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | ACCEPT | Summary: The purified kinase assay directly supports EGFR catalytic activity toward PCNA. Reason: The purified kinase assay directly supports EGFR catalytic activity toward PCNA. The source-specific account distinguishes commercial GSTβEGFR kinase-domain assays from nuclear fractionation, confocal localization and EGF-responsive cellular experiments. This catalytic-domain/substrate claim remains protein tyrosine kinase activity; it is not evidence for a complete ligand-binding transmembrane receptor reaction in the nuclear assay. PCNA Tyr211-dependent stability is supported by proteasome-inhibition rescue and equal-amount repair comparisons; this does not confer PCNA repair or polymerase chemistry on EGFR. The available original text comprises selected Results/Figure 6 and operative Methods windows plus official S1βS3 captions, not a complete downloaded paper or inspected figure pixels. Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | ACCEPT | Summary: The integrated ligand-response context supports receptor activity; isolated nuclear catalysis alone would be insufficient. Reason: The integrated ligand-response context supports receptor activity; isolated nuclear catalysis alone would be insufficient. The source-specific account distinguishes commercial GSTβEGFR kinase-domain assays from nuclear fractionation, confocal localization and EGF-responsive cellular experiments. PCNA Tyr211-dependent stability is supported by proteasome-inhibition rescue and equal-amount repair comparisons; this does not confer PCNA repair or polymerase chemistry on EGFR. The available original text comprises selected Results/Figure6 and operative Methods windows plus official S1βS3 captions, not a complete downloaded paper or inspected figure pixels. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: Nuclear EGFR associates with PCNA in the studied cancer-cell context. Reason: The independently recovered PMID:17115032 operative text and official supplementary captions support nuclear EGFRβPCNA coimmunoprecipitation, alongside separate kinase and protein-stability assays. This positive association is retained. PCNA is a sliding-clamp component, not itself the DNA polymerase or a repair enzyme, so generic enzyme or polymerase binding is not inferred from its partners. The commercial GST-EGFR kinase-domain assay has unverified exact insert bounds; it does not establish that every natural EGFR product shares the nuclear interaction. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: Nuclear fractionation and confocal localization support this context-dependent pool; this source is not a transcription-factor assay. Reason: Nuclear fractionation and confocal localization support this context-dependent pool; this source is not a transcription-factor assay. The source-specific account distinguishes commercial GSTβEGFR kinase-domain assays from nuclear fractionation, confocal localization and EGF-responsive cellular experiments. PCNA Tyr211-dependent stability is supported by proteasome-inhibition rescue and equal-amount repair comparisons; this does not confer PCNA repair or polymerase chemistry on EGFR. The available original text comprises selected Results/Figure6 and operative Methods windows plus official S1βS3 captions, not a complete downloaded paper or inspected figure pixels. Supporting Evidence: |
| GO:0042177 negative regulation of protein catabolic process | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: PCNA Tyr211 phosphorylation protects chromatin-associated PCNA from degradation. Reason: PCNA Tyr211 phosphorylation protects chromatin-associated PCNA from degradation. The source-specific account distinguishes commercial GSTβEGFR kinase-domain assays from nuclear fractionation, confocal localization and EGF-responsive cellular experiments. PCNA Tyr211-dependent stability is supported by proteasome-inhibition rescue and equal-amount repair comparisons; this does not confer PCNA repair or polymerase chemistry on EGFR. The available original text comprises selected Results/Figure6 and operative Methods windows plus official S1βS3 captions, not a complete downloaded paper or inspected figure pixels. Supporting Evidence: |
| GO:0045739 positive regulation of DNA repair | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: The source supports positive regulation of repair through PCNA stability, not EGFR executing repair chemistry. Reason: The source supports positive regulation of repair through PCNA stability, not EGFR executing repair chemistry. The source-specific account distinguishes commercial GSTβEGFR kinase-domain assays from nuclear fractionation, confocal localization and EGF-responsive cellular experiments. PCNA Tyr211-dependent stability is supported by proteasome-inhibition rescue and equal-amount repair comparisons; this does not confer PCNA repair or polymerase chemistry on EGFR. The available original text comprises selected Results/Figure6 and operative Methods windows plus official S1βS3 captions, not a complete downloaded paper or inspected figure pixels. Supporting Evidence: |
| GO:0045740 positive regulation of DNA replication | IDA PMID:17115032 Tyrosine phosphorylation controls PCNA function through prot... | KEEP AS NON CORE | Summary: The source supports positive regulation of replication through PCNA stability, not EGFR acting as a polymerase. Reason: The source supports positive regulation of replication through PCNA stability, not EGFR acting as a polymerase. The source-specific account distinguishes commercial GSTβEGFR kinase-domain assays from nuclear fractionation, confocal localization and EGF-responsive cellular experiments. PCNA Tyr211-dependent stability is supported by proteasome-inhibition rescue and equal-amount repair comparisons; this does not confer PCNA repair or polymerase chemistry on EGFR. The available original text comprises selected Results/Figure6 and operative Methods windows plus official S1βS3 captions, not a complete downloaded paper or inspected figure pixels. Supporting Evidence: |
| GO:0019899 enzyme binding | IPI PMID:12009895 Plasma membrane phospholipid scramblase 1 is enriched in lip... | KEEP AS NON CORE | Summary: EGFR associates with the catalytic protein PLSCR1. Reason: The recovered original uses reciprocal immunoprecipitation in human KB cells and distinguishes association from proof of a purified binary interface or direct EGFR phosphorylation of PLSCR1. The current official O15162 record documents catalytic phospholipid scrambling and nuclease activity with experimental provenance. Enzyme binding is therefore supported as an accessory partner-class interaction; EGFR is not assigned either PLSCR1 activity. Supporting Evidence: |
| GO:0045121 membrane raft | IDA PMID:12009895 Plasma membrane phospholipid scramblase 1 is enriched in lip... | ACCEPT | Summary: EGFR is enriched in operationally defined membrane raft fractions. Reason: The original human KB-cell study uses both detergent-free and detergent-containing fractionation, flotillin/transferrin-receptor controls and cholesterol depletion. EGFR follows the raft-associated distribution in these assays. This supports membrane raft localization without claiming every surface receptor occupies a fixed raft or equating co-fractionation with direct binding. Supporting Evidence: |
| 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 contributes to serum-dependent protection against apoptosis in the tested cell context. Reason: Figure 5 tests EGFR directly: neutralizing antibody Ab528B attenuates serum protection against TNF-alpha/cycloheximide-induced apoptosis in SW13 cells, with DNA-fragmentation measurements and parallel receptor-phosphorylation controls. This supports the negative apoptotic-process sign beyond the separate SPRY2 perturbations. Retain the contextual signaling role without making universal survival claims or treating the mouse c-Cbl experiments as human EGFR construct assays. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17182860 Activated Cdc42-associated kinase 1 is a component of EGF re... | MODIFY | Summary: EGFR physically associates with the protein kinase ACK1/TNK2. Reason: The original Methods identify the mouse ACK1 construct, matching imported O54967. Co-immunoprecipitation and a GST ACK1 binding-region pull-down support association with EGFR; separate human-cell experiments also recover endogenous complexes. Protein kinase binding describes the partner class. The pull-down uses cell lysate, and the authors discuss possible adaptor-mediated contact rather than a purified binary interface. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005768 endosome | IDA PMID:17182860 Activated Cdc42-associated kinase 1 is a component of EGF re... | ACCEPT | Summary: EGFR is observed in endosomal vesicles in the ACK1 study. Reason: Figure7 and the operative Results show EGFR with GFP-ACK1 on vesicles associated with the EEA1 marker after EGF stimulation. This imaging uses COS7 cells and the mouse ACK1 construct; it is not direct human-cell microscopy. The conserved endosomal pool is consistent with independently established human EGFR trafficking, without asserting that all receptor-containing vesicles have the same subtype. |
| GO:0004888 transmembrane signaling receptor activity | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | MODIFY | Summary: The reported receptor activity can be specified as EGFR activity. Reason: Although the paper foregrounds interleukin-2 signaling, its complete abstract explicitly discusses the EGF receptor pathway in the hematopoietic-cell signaling comparison. Together with the independently supported ligand-responsive EGFR function, this supports the specific receptor term rather than the broad transmembrane receptor category. The original EGFR construct, host details and operative assay controls were unavailable; no wrong-gene attribution is inferred from the title. Proposed replacements: epidermal growth factor receptor activity |
| GO:0007166 cell surface receptor signaling pathway | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | MODIFY | Summary: The source explicitly includes an EGF receptor signaling pathway comparison. Reason: The complete abstract names the EGF receptor pathway while comparing signaling routes that support cell-cycle progression in the hematopoietic model. The specific EGFR signaling term is more informative than generic cell-surface receptor signaling. This source-level interpretation does not claim that the unavailable full Methods established the same signaling intermediates in every receptor system. Proposed replacements: epidermal growth factor receptor signaling pathway Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | ACCEPT | Summary: The source explicitly addresses EGFR signaling in the growth-signaling comparison. Reason: The complete abstract discusses EGFR signaling as a pathway converging with a growth-promoting route in the hematopoietic model. This is compatible with the curated EGFR-pathway assertion and the receptor's independently established function. The paper's emphasis on interleukin-2 does not establish a citation error; original EGFR-specific Methods were unavailable. Supporting Evidence: |
| GO:0008284 positive regulation of cell population proliferation | IDA PMID:7736574 Three distinct IL-2 signaling pathways mediated by bcl-2, c-... | ACCEPT | Summary: The curated proliferation assertion agrees with EGFRβs established mitogenic signaling role. Reason: The abstract discusses signaling combinations that support cell-cycle progression and explicitly compares the EGF receptor pathway with a growth-promoting route. The curated positive-proliferation assertion agrees with the principal mitogenic role independently supported by human EGFR depletion in PMID:27057632. Exact EGFR-specific proliferation experiments in PMID:7736574 could not be reconstructed from the unavailable original body; acceptance does not claim those Methods or add an assay or species attribution. |
| 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 enhances beta-catenin/TCF output in the studied oral-cancer cells. Reason: EGF stimulation, EGFR inhibition and Erbitux treatment alter beta-catenin localization and TOP/FOP reporter output in SAS and OECM1 cells. These experiments support positive modulation of the canonical beta-catenin signaling output. Retain this contextual cross-talk annotation without making EGFR a Wnt receptor, claiming a direct purified EGFR-to-GSK3 reaction, or generalizing the phenotype to every tissue. The experiments did not directly test a Wnt-ligand requirement. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:17599051 The evolutionarily conserved EBR module of RALT/MIG6 mediate... | ACCEPT | Summary: The RALT study directly addresses EGFR catalytic activity. Reason: The complete abstract reports inhibition of EGFR kinase activity in vitro and in intact cells by the RALT/MIG6 EBR module, with a mapped receptor kinase-region interaction. This supports tyrosine-kinase activity at the stated assay scope. Full Methods were unavailable, so precise preparation identity and kinetics are not reconstructed. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17599051 The evolutionarily conserved EBR module of RALT/MIG6 mediate... | KEEP AS NON CORE | Summary: EGFR binds the RALT/MIG6 feedback inhibitor. Reason: The complete abstract reports EBR-dependent binding and inhibition of EGFR. The exact imported P05432 record identifies rat ERRFI1/RALT and independently cites this interaction. The supported association is retained under the project-specific generic-binding policy; an inhibitor is not automatically a catalytic enzyme partner, and the source does not establish a homogeneous native human complex. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:7588596 WT1 suppresses synthesis of the epidermal growth factor rece... | ACCEPT | Summary: EGFR staining includes a cytoplasmic pool in developing human kidney. Reason: Original Figure6b explicitly identifies cytoplasmic EGFR immunostaining in frozen sections of 13-week human kidney. The Methods specify anti-EGFR monoclonal antibody528 and nuclear counterstaining; rat developmental RNA measurements in Figure6a are a separate experiment. The cytoplasmic annotation is therefore supported by target-specific human staining, rather than inferred merely from the topology of the intracellular kinase domain. The staining does not resolve a particular cytoplasmic organelle or natural isoform, and basolateral membrane staining in differentiating tubules is also reported. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19602593 Cetuximab/C225-induced intracellular trafficking of epiderma... | MODIFY | Summary: EGFR associates with the SEC61 transmembrane transporter complex. Reason: PMID:19602593 immunoprecipitation Methods and Fig. 4 demonstrate EGFR recovery with Sec61Ξ² in C225-treated MDA-MB-468 and DiFi cells. SEC61B is an established subunit of the SEC61 channel-forming transporter complex. GO:0044325 explicitly includes binding to a transporter protein complex, supporting this more informative partner class. The assay establishes complex association, not a purified EGFRβSEC61B interface; it also does not assign transporter activity to EGFR or generalize the antibody-induced trafficking state to every receptor pool. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0070435 Shc-EGFR complex | ISS GO_REF:0000024 | ACCEPT | Summary: The original establishes a ligand-induced ShcβEGFR complex in rat cells. Reason: Current Q9QX70 is rat EGFR and its exact GO:0070435 IDA cites PMID:7513704. The original Methods and Results/Figure 1 report anti-Shc immunoprecipitation recovering phosphorylated EGFR after EGF stimulation in Rat1-derived cells. The human transgene in those cells is the insulin receptor; endogenous EGFR must not be described as a human construct. The human Shc SH2 fusion is a separate reagent. These data support the conserved signaling-complex assertion without equating co-immunoprecipitation with a purified interface or assigning a particular human EGFR isoform. |
| GO:0019903 protein phosphatase binding | IPI PMID:15899872 Transforming growth factor {beta} (TGF-{beta})-Smad target g... | KEEP AS NON CORE | Summary: EGFR associates with the receptor protein tyrosine phosphatase PTPRK in the reported signaling context. Reason: The literal imported partner is Q15262/PTPRK. The abstract reports endogenous association with EGFR, and the Discussion connects this phosphatase to reduced ErbB signaling. Official human Q15262 independently verifies the phosphatase class. Keep this regulatory interaction as non-core; it neither gives EGFR phosphatase activity nor establishes a purified binary interface. The current binding children distinguish PP1, PP2A, PP2B and PP5 and do not provide a supported PTPRK-specific refinement. Replace the inherited rationale naming unrelated PTPN proteins. Supporting Evidence: |
| 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 participates in a keratinocyte response to UVA. Reason: The available article text reports low, nonlethal UVA exposure in human HaCaT keratinocytes, EGFR/AKT activation and cyclin D1 induction, with EGFR inhibition and upstream ADAM17 perturbation. Its retained abstract and Discussion contain these positive results, although the cached text omits the operative Methods and Results sections. The response is experimentally reported; its contextual disposition does not imply the irradiation response is biologically false or that EGFR is a photosensor. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17909029 The phosphoinositide kinase PIKfyve mediates epidermal growt... | MODIFY | Summary: EGFR physically associates with the kinase PIKFYVE during nuclear trafficking. Reason: The source reports PIKFYVE in EGFR immune complexes from human TCCSUP cells and discusses their co-immunoprecipitation as a cytosolic complex associated with nuclear trafficking. The captured official PIKFYVE record documents both lipid-kinase chemistry and serine-protein kinase activity, so the protein-kinase partner class is supported independently of its name. Co-purification does not establish a purified interface or transfer PIKFYVE chemistry to EGFR. The available original cache contains the abstract and Discussion but omits operative Results/Methods; that access limit is preserved. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0016323 basolateral plasma membrane | IDA PMID:12646923 Segregation of receptor and ligand regulates activation of e... | KEEP AS NON CORE | Summary: EGFR is present at the basolateral membrane of differentiated human airway epithelial cells. Reason: The publisher original Figure 2d and its caption explicitly identify erbB1 at the basolateral membrane in human airway epithelia. This directly supports the imported cellular-component annotation despite the abstract foregrounding erbB2β4. It is retained as a polarized-epithelial localization context, consistently with the ortholog-based basolateral row, rather than implying universal basolateral residence. The full operative Methods were not recovered, so antibody specificity and complete culture details were not independently audited. The heregulin-dependent phosphorylation and wound-healing experiments foreground other ErbB receptors and are not transferred to EGFR. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11279102 Sorting nexin 6, a novel SNX, interacts with the transformin... | KEEP AS NON CORE | Summary: Transfected SNX6 and EGFR coassociate in cells. Reason: PMID:11279102 Results and Fig. 3 explicitly show HA-SNX6 recovery after immunoprecipitation of transfected EGFR in COS-7 cells, with receptor and SNX6 expression controls. Methods establish the human full-length SNX6 clone; the inspected text does not independently resolve the receptor insert sequence or natural isoform. This is positive receptor-complex evidence rather than purified direct contact. SNX6 trafficking and membrane-remodeling roles do not supply an evidence-backed narrower binding class here. Retain the generic positive interaction as non-core under the project instruction. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1225978 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1225978 (Covalent tyrosine kinase inhibitors bind and inhibit wild-type EGF:EGFR dimers), the captured typed path 1225978 --input--> 9624420; 9624420 --hasComponent--> 9624419; 9624419 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1225978 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1248677 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1248677 (Inactivation of over-expressed wild type EGFR by Cetuximab recombinant antibody), the captured typed path 1248677 --input--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1248677 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177922 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177922 (EGFR dimerization), the captured typed path 177922 --input--> 9624419; 9624419 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177922 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-177942 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-177942 (EGFR binds EGF ligand), the captured typed path 177942 --input--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-177942 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963586 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1963586 (SRC family kinases phosphorylate ERBB2), the captured typed path 1963586 --input--> 1963573; 1963573 --hasMember--> 1227939; 1227939 --hasComponent--> 179847; 179847 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1963586 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1963589 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1963589 (ERBB2 forms heterodimers with ligand-activated ERBB receptors: EGFR, ERBB3 and ERBB4), the captured typed path 1963589 --input--> 1963571; 1963571 --hasMember--> 179847; 179847 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1963589 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-1977959 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-1977959 (ERBB4 forms heterodimers with EGFR), the captured typed path 1977959 --input--> 179847; 179847 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-1977959 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-445069 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-445069 (L1-EGFR trans-heterodimerization), the captured typed path 445069 --input--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-445069 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857549 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8857549 (HBEGF-bound EGFR forms a heterodimer with GPNMB), the captured typed path 8857549 --input--> 8857547; 8857547 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8857549 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857555 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8857555 (EGFR phosphorylates GPNMB), the captured typed path 8857555 --input--> 8857546; 8857546 --hasComponent--> 8857547; 8857547 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8857555 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857565 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8857565 (Phosphorylated GPNMB recruits PTK6 and LRRK2 in the presence of LINC01139), the captured typed path 8857565 --input--> 8857556; 8857556 --hasComponent--> 8857547; 8857547 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8857565 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857577 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8857577 (LINC01139 facilitates PTK6 autophosphorylation), the captured typed path 8857577 --input--> 8857567; 8857567 --hasComponent--> 8857556; 8857556 --hasComponent--> 8857547; 8857547 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8857577 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8857583 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8857583 (LINC01139 promotes phosphorylation of HIF1A by PTK6), the captured typed path 8857583 --catalystActivity--> 8857582; 8857582 --physicalEntity--> 8857574; 8857574 --hasComponent--> 8857556; 8857556 --hasComponent--> 8857547; 8857547 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8857583 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8874797 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-8874797 (EGFR gene expression is stimulated by TFAP2C), the captured typed path 8874797 --output--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-8874797 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9609689 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9609689 (HCMV Binds to the Host Cell via heparan sulfate proteoglycans (HSPG)), the captured typed path 9609689 --input--> 9610864; 9610864 --hasMember--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9609689 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9610867 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9610867 (HCMV Binds Host Cell Receptor - Endocytic Pathway), the captured typed path 9610867 --input--> 9610864; 9610864 --hasMember--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9610867 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9611147 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9611147 (Endocytic Uptake of HCMV Virion), the captured typed path 9611147 --input--> 9609688; 9609688 --hasComponent--> 9610864; 9610864 --hasMember--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9611147 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9611158 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9611158 (Fusion of HCMV Envelope with Plasma Membrane), the captured typed path 9611158 --output--> 9610864; 9610864 --hasMember--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9611158 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9634702 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9634702 (LINC01139 promotes phosphorylation of HIF1A by LRRK2), the captured typed path 9634702 --catalystActivity--> 9634703; 9634703 --physicalEntity--> 8857574; 8857574 --hasComponent--> 8857556; 8857556 --hasComponent--> 8857547; 8857547 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9634702 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9664567 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9664567 (ERBB2 KD mutants heterodimerize), the captured typed path 9664567 --input--> 9667208; 9667208 --hasMember--> 9646489; 9646489 --hasMember--> 179847; 179847 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9664567 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665388 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665388 (ERBB2 ECD mutants heterodimerize with EGFR), the captured typed path 9665388 --input--> 179847; 179847 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665388 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9665697 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9665697 (ERBB2 TMD/JMD mutants hetrodimerize), the captured typed path 9665697 --input--> 9646489; 9646489 --hasMember--> 179847; 179847 --hasComponent--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. The disease-marked event includes this non-disease-marked EGFR reference entity; a disease flag on the overall event does not establish that EGFR itself is mutant. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9665697 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9674531 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9674531 (AAMP binds EGFR), the captured typed path 9674531 --input--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9674531 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9851407 | ACCEPT | Summary: Retain plasma membrane with the exact EGFR entity and event scope. Reason: In R-HSA-9851407 (FAM83B, (FAM83A, FAM83D) bind EGFR), the captured typed path 9851407 --input--> 179837 reaches human EGFR entity 179837 (EGFR [plasma membrane]), whose reference entity is UniProt P00533. The EGFR entity itself carries GO:0005886; this location is not inferred solely from the event compartment. This is an independently traced curated model; no additional original-paper assay or complete closure of every alternative branch is claimed. Supporting Evidence: Reactome:R-HSA-9851407 |
| GO:0007165 signal transduction | IDA PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | MODIFY | Summary: The source examines EGFR signaling in human bronchial epithelial derivatives. Reason: The source abstract explicitly connects TGF-alpha/EGFR and EGFR-containing ERBB heterodimers to MAPK signaling in the epithelial models, including receptor trapping or surface blockade. EGFR signaling is more informative than generic signal transduction. The detailed original Methods were unavailable, so exact engineered receptor boundaries are not asserted. Proposed replacements: epidermal growth factor receptor signaling pathway 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 supports growth-related behavior in the bronchial epithelial tumor model. Reason: The complete abstract links TGF-alpha/EGFR signaling and altered ERBB heterodimers to tumorigenic behavior of the human bronchial epithelial derivatives, with receptor-directed perturbations. This is compatible with the curator's positive epithelial-proliferation assertion and is retained as a contextual phenotype. The original growth-assay details were unavailable and are not reconstructed from tumorigenicity alone. 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... | MODIFY | Summary: EGFR binds the growth factor epiregulin. Reason: The authentic PMID:9419975 abstract describes radiolabeled epiregulin crosslinking to EGFR and ERBB4 in human breast-cancer cell lines, while the other ERBB receptors show distinct binding and phosphorylation behavior. This positive ligand-binding result supports growth-factor binding as the informative class. Complete operative Methods and experimental ligand/receptor product sequences were not recovered; ERBB4 binding or downstream phosphorylation of other receptors is not reassigned to EGFR. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:2176151 The tyrosine phosphorylated carboxyterminus of the EGF recep... | MODIFY | Summary: Phosphorylated EGFR directly binds the tested GAP SH2-containing region. Reason: The complete original tests a bacterial TRP-E fusion containing GAP171β448 and phosphorylated EGFR intracellular/carboxy-terminal preparations, with unphosphorylated and TRP-E controls. This directly grounds SH2 domain binding rather than an inferred interaction with every GAP domain. The exact imported RASA1 identity remains unchanged. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0004709 MAP kinase kinase kinase activity | NAS PMID:15542601 Activation of the epidermal growth factor receptor by respir... | REMOVE | Summary: EGFR-dependent ERK signaling does not make EGFR a MAP kinase kinase kinase. Reason: GO:0004709 requires phosphorylation and activation of a MAP kinase kinase. The separately recovered original Methods and Figure 4/Results use human A549 cells, EGFR inhibition or siRNA, phospho-ERK immunoblots and IL-8 measurements. They establish upstream EGFR receptor signaling, not the MAP3K catalytic step. EGFR is the receptor tyrosine kinase in this pathway, rather than its MAP kinase kinase kinase. Remove the incorrect catalytic assignment while preserving the positive MAPK/ERK process annotations, including GO:0070374. This conclusion uses the operative experiments and pathway role, not missing full text or an abstract-only absence. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | IMP PMID:14702346 Sorting of ligand-activated epidermal growth factor receptor... | MODIFY | Summary: The sorting study tests kinase-dependent signaling by ligand-responsive EGFR. Reason: The original uses human wild-type, K721A and actin-binding-region deletion constructs in NIH3T3 cells to examine EGF-dependent receptor trafficking. EGFR activity is the more informative intact-receptor function in this experiment. The mutant comparison does not transfer receptor kinase activity to actin or establish activity of natural truncated products. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | ACCEPT | Summary: The human EGFR construct retains ligand-binding and receptor-kinase function. Reason: The original Results report specific radiolabeled EGF binding and EGF-dependent phosphorylation of the expressed receptor in human esophageal keratinocytes. These measurements support epidermal growth factor receptor activity. They do not establish equivalent function for every natural truncated product. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:12828935 Activation of epidermal growth factor receptor signals induc... | KEEP AS NON CORE | Summary: A nuclear phosphorylated-EGFR pool is reported in the astrocyte context. Reason: The complete abstract explicitly describes nuclear phosphorylated EGFR after hydrostatic-pressure stimulation in optic-nerve-head astrocytes. This positive source-specific localization is retained without implying universal nuclear residence or direct sequence-specific DNA binding. The original imaging and fractionation Methods were not recovered. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | ACCEPT | Summary: EGFR staining includes a cytoplasmic pool in the keratinocyte model. Reason: The original Results explicitly describe both membrane staining and diffuse cytoplasmic EGFR staining in the human keratinocyte constructs. This supports the broad cytoplasmic compartment without implying soluble cytosolic topology or an exclusively cytoplasmic receptor. Supporting Evidence: |
| GO:0005768 endosome | IDA PMID:14702346 Sorting of ligand-activated epidermal growth factor receptor... | ACCEPT | Summary: Human EGFR constructs are followed through endosomal compartments. Reason: The original Methods and Results combine ligand uptake/degradation measurements, fractionation and microscopy in NIH3T3 cells expressing human EGFR constructs. They support endosomal localization while distinguishing early internalization from later lysosomal sorting. The mouse host does not change the stated human identity of the expressed receptor. Supporting Evidence: |
| GO:0016020 membrane | IDA PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | MODIFY | Summary: The receptor is detected at the plasma membrane in the keratinocyte model. Reason: The original membrane immunostaining, cell-surface radioligand binding and EGFR/p120 confocal localization support plasma-membrane localization more specifically than membrane. Other cytoplasmic staining in the same experiment is preserved as a nonexclusive pool. Proposed replacements: plasma membrane Supporting Evidence: |
| 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 keratinocyte migration in the measured assay. Reason: The original haptotactic migration assay uses primary human esophageal keratinocytes and reports increased migration with EGFR expression and EGF; AG1478 reduces the response. EGFR therefore contributes actively through signaling, rather than merely marking migrating cells. This is a contextual cellular output, not a separate motor activity. Supporting Evidence: |
| GO:0050730 regulation of peptidyl-tyrosine phosphorylation | IMP PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | KEEP AS NON CORE | Summary: EGFR activation regulates downstream tyrosine phosphorylation in keratinocytes. Reason: The original Results measure receptor phosphorylation and STAT1 tyrosine phosphorylation after EGF stimulation in the human keratinocyte system. These support regulation of tyrosine phosphorylation. A cellular downstream phosphosite readout does not by itself identify EGFR as the direct kinase for every measured substrate. Supporting Evidence: |
| GO:0051015 actin filament binding | IDA PMID:14702346 Sorting of ligand-activated epidermal growth factor receptor... | KEEP AS NON CORE | Summary: EGFR actin association is retained with its experimental provenance distinguished. Reason: The recovered original discusses prior direct F-actin-binding and peptide-competition experiments, then tests an EGFR actin-binding-region deletion in sorting assays. The authors explicitly leave open other functions of the deleted region. Actin binding is retained as a supported accessory interaction; the 2004 sorting phenotype is not presented as a new purified actin-binding assay or proof that actin contact alone controls sorting. Supporting Evidence: |
| GO:0051205 protein insertion into membrane | TAS PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | MODIFY | Summary: EGFR promotes recruitment of p120-catenin to the plasma membrane. Reason: GO:0051205 requires incorporation into the hydrophobic region of a lipid bilayer. The original fractionation and confocal experiments instead show p120-catenin redistribution from cytosol to plasma membrane and stronger association with E-cadherin. Positive regulation of protein localization to plasma membrane describes this measured outcome without converting peripheral recruitment into membrane insertion. Proposed replacements: positive regulation of protein localization to plasma membrane Supporting Evidence: |
| GO:0098609 cell-cell adhesion | IMP PMID:12435727 Epidermal growth factor receptor mediates increased cell pro... | MODIFY | Summary: EGFR signaling increases E-cadherin-dependent cell aggregation. Reason: The original rotary aggregation assay reports an EGF-dependent increase that is blocked by EGFR inhibition and by a neutralizing E-cadherin antibody. Together with p120 recruitment and E-cadherin association, this supports positive regulation of cell-cell adhesion. The experiments do not identify EGFR itself as the molecule forming the adhesive bond between the cells. Proposed replacements: positive regulation of cell-cell adhesion Supporting Evidence: |
| GO:0001503 ossification | NAS PMID:12925580 Mice humanised for the EGF receptor display hypomorphic phen... | KEEP AS NON CORE | Summary: EGFR contributes to bone development in a human-receptor knock-in mouse model. Reason: The authentic abstract reports human EGFR cDNA replacement in mice, low expression in bone cells and accelerated chondrocyte/osteoblast differentiation, also seen in Egfr-null mice. Selected indexed original Methods describe neonatal mouse calvarial cultures and bone-nodule assays. This supports retaining the curator-supplied NAS ossification annotation as a developmental role, without claiming an experiment in human bone or direct matrix synthesis. The complete bone Results and figure data were not recovered. The separately identified correction concerns a duplicated heart-image panel in Figure 6; it is not evidence that the bone finding was withdrawn. Supporting Evidence: |
| GO:0005615 extracellular space | NAS PMID:9103388 Expression of a truncated epidermal growth factor receptor-l... | UNDECIDED | Summary: Extracellular localization of the cited truncated EGFR product remains unresolved. Reason: The complete authentic abstract establishes TEGFR expression in human ovarian cancer and relates it to the previously described placental product. It does not establish secretion, extracellular detection, or the exact natural product sequence, and the operative original was not recovered. Truncation alone is insufficient to identify a secreted isoform. Current QuickGO marks GO:0005615 obsolete as the same concept as GO:0005576; that ontology update does not resolve the biological evidence or justify rewriting this imported source identifier. Supporting Evidence: |
| GO:0042327 positive regulation of phosphorylation | IDA PMID:15082764 Epidermal growth factor receptor stimulation activates the R... | MODIFY | Summary: EGFR signaling promotes phosphorylation-dependent activation of CUG-BP1 in mammary epithelial cells. Reason: The abstract and Discussion identify increased phosphorylation of the protein CUG-BP1 following EGFR stimulation, supporting the protein-specific child of the imported phosphorylation term. The Discussion places MAPK signaling between receptor stimulation and CUG-BP1 regulation; it does not establish purified EGFR directly phosphorylating CUG-BP1. Retain the positive regulatory claim with this narrower substrate class. Proposed replacements: positive regulation of protein phosphorylation Supporting Evidence: |
| GO:0003690 double-stranded DNA binding | NAS PMID:6325948 ATP-stimulated interaction between epidermal growth factor r... | UNDECIDED | Summary: The source reports a positive purified-receptor interaction with double-stranded DNA; its detailed assay basis remains unresolved. Reason: The complete primary abstract explicitly reports ATP-stimulated interaction with and nicking of supercoiled double-stranded DNA by a purified EGF-receptor preparation. That report is relevant to the actual GO:0003690 definition, binding to double-stranded DNA, and cannot be replaced by a rationale about indirect transcription-factor association. The publisher PDF route returned only a subscription-preview HTML page, so the purification, assay controls and receptor preparation could not be independently assessed. Retain source-specific uncertainty without asserting that the experiment was negative, contaminated or misattributed; no separate nuclease activity is proposed. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | TAS PMID:16076471 The epidermal growth factor receptors and their family of li... | MODIFY | Summary: The review describes ligand-activated EGFR receptor tyrosine kinase function. Reason: The complete review abstract identifies the EGF receptor as a type-I receptor with tyrosine kinase activity activated by cognate ligand binding. For this intact receptor context, epidermal growth factor receptor activity is a more informative term than generic protein tyrosine kinase activity. This is a traceable author-statement source, not a newly reconstructed direct enzyme experiment, and it does not attribute full receptor signaling to every truncated natural product. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | NAS PMID:2790960 Functional independence of the epidermal growth factor recep... | ACCEPT | Summary: EGFR transduces ligand binding through its intrinsic receptor tyrosine kinase. Reason: The source abstract distinguishes kinase-active, internalization-defective receptors from kinase-inactive receptors and reports ligand-dependent mitogenic signaling by the former. This directly fits the receptor function at the stated abstract-level scope. It does not establish that endocytosis and catalytic signaling are the same mechanistic step, nor does it identify a natural alternative product. Supporting Evidence: |
| GO:0005006 epidermal growth factor receptor activity | NAS PMID:6325948 ATP-stimulated interaction between epidermal growth factor r... | ACCEPT | Summary: The source identifies EGFR as an EGF-responsive transmembrane tyrosine-kinase receptor. Reason: The verified abstract identifies the EGF receptor and EGF-enhanced receptor kinase activity, consistent with the established receptor molecular function. Its reported DNA-interaction experiment is a separate claim and does not negate that receptor identity. The unavailable original body limits reconstruction of that experiment; this NAS receptor assertion is not presented as a newly reconstructed ligand-binding or natural-isoform assay. Supporting Evidence: PMID:6325948 The receptor for epidermal growth factor (EGF) has been identified as a transmembrane glycoprotein that has tyrosine-specific kinase activity. |
| GO:0005886 plasma membrane | IDA PMID:15465819 Ubiquitin ligase activity of c-Cbl guides the epidermal grow... | ACCEPT | Summary: The source supports plasma-membrane localization of EGFR before coated-pit internalization. Reason: The complete abstract explicitly describes recruitment at the plasma membrane and entry of ligand-bound EGFR into coated pits and vesicles. This agrees with the imported experimental localization. The unavailable full body limits reconstruction of the exact cell and construct provenance, but does not contradict the directly stated localization or justify rejecting the curated positive. Supporting Evidence: PMID:15465819 Both the ubiquitin ligase activity of c-Cbl and the UIM of Eps15 were necessary for plasma membrane recruitment of Eps15 and entry of ligand-bound EGFR into coated pits and vesicles containing Eps15. |
| GO:0018108 peptidyl-tyrosine phosphorylation | IEA | NEW | Summary: EGFR directly catalyzes phosphorylation of tyrosine residues in protein substrates. Reason: Retain this inherited proposal for the chemical step performed by EGFR. PMID:27872189 reports recombinant human EGFR kinase-domain phosphorylation of EGFR and HER3 tail constructs, detected with phosphotyrosine antibodies and distinguished from no-kinase and no-tail controls. EGFR therefore performs the phosphorylation reaction rather than merely being required for its outcome. Current typed ontology closure does not make GO:0018108 an ancestor or descendant of the other inherited proposal or any imported EGFR term; GO:0005006 is a receptor molecular function, not this biological-process assertion. Same-role receptors ERBB2 and PDGFRA carry experimental peptidyl-tyrosine phosphorylation annotations. The inherited IEA field is preserved as historical proposal metadata, not represented as a newly obtained computational annotation. Construct-specific chemistry does not establish activity of every natural EGFR product. Supporting Evidence: PMID:6325948 The kinase activity of the receptor is enhanced in the presence of EGF (or related peptides), and the phosphorylation of a number of substrates, as well as autophosphorylation of the receptor, has been reported. |
| GO:0046777 protein autophosphorylation | IEA | NEW | Summary: EGFR phosphorylates its own cytoplasmic tail, generating signaling-protein docking sites. Reason: Retain this inherited proposal with a distinction between tail phosphorylation and kinase activation. EGFR performs the phosphate-transfer step on its own protein sequence; this is participation rather than evidence based solely on receptor necessity. PMID:27872189 directly measures EGFR kinase-domain phosphorylation of an EGFR tail construct and reports an intracellular-half phosphorylation positive control. The separate-domain reaction establishes sequence-specific chemistry; it is not by itself a measurement of full-length receptor dimer geometry. Tail phosphorylation supplies docking sites after kinase activation and should not be equated with the asymmetric allosteric activation mechanism. Current is_a/part_of closure does not make GO:0046777 an ancestor or descendant of an imported term or GO:0018108, and same-role KIT and PDGFRA carry experimental autophosphorylation annotations. The historical source fields and original supporting excerpt remain unchanged; no universal isoform-equivalence or quantitative kinetic claim is made. Supporting Evidence: file:human/EGFR/EGFR-uniprot.txt Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. |
| GO:0005006 epidermal growth factor receptor activity | IDA PMID:12828935 Activation of epidermal growth factor receptor signals induc... | ACCEPT | Summary: EGFR activity is implicated in the optic-nerve-head astrocyte response. Reason: The complete source abstract reports activation of EGFR in human optic-nerve-head astrocytes and connects it to NOS2 induction in vitro and in glaucomatous tissue. This supports the established receptor function at the source's stated scope. The unavailable original Methods do not establish a particular natural isoform or purified enzyme kinetics. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10026169 Identification of Grb4/Nckbeta, a src homology 2 and 3 domai... | UNDECIDED | Summary: Human NCK1 SH2 binding is measured against mouse-cell receptor material. Reason: PMID:10026169 specifies a human NCK1 SH2 fragment, residues 275β377, and positive receptor-associated pull-down from mouse embryonic fibroblast lysate. The human EGFR target behind this imported IPI row was not authenticated. This is a source-mapping uncertainty, not a claim that EGFRβNCK1 binding is false or that a purified interface is required. Leave UNDECIDED; GO:0042169 is a conditional domain-level refinement once the human-target attribution is resolved. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10026169 Identification of Grb4/Nckbeta, a src homology 2 and 3 domai... | UNDECIDED | Summary: Human GRB2 SH2 binding is measured against mouse-cell receptor material. Reason: PMID:10026169 uses a human GRB2 SH2 fragment, residues 57β154, with mouse embryonic fibroblast receptor lysate. The inspected source does not establish a human EGFR transgene. Keep this exact human-target IPI attribution undecided while preserving the positive cross-species domain evidence. This does not dispute established EGFRβGRB2 biology or imply that every GRB2 isoform binds EGFR. GO:0042169 is the conditional refinement if target provenance is resolved. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | MODIFY | Summary: EGFR associates with ERBB3 in the human bronchial epithelial model. Reason: The complete source abstract reports distinct EGFR heterodimers in human immortalized bronchial epithelial derivatives, and the literal interaction record maps the exact human EGFRβERBB3 pair to anti-bait co-immunoprecipitation. The independently captured official partner record supports the receptor class. This refinement characterizes the associated partner without claiming a purified interface or applying the same heterodimer composition to both cell derivatives. The original full Methods and insert sequence were unavailable. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10572067 Dominance of ErbB-1 heterodimers in lung epithelial cells ov... | MODIFY | Summary: EGFR associates with ERBB4 in the human bronchial epithelial model. Reason: The complete source abstract reports distinct EGFR heterodimers in human immortalized bronchial epithelial derivatives, and the literal interaction record maps the exact human EGFRβERBB4 pair to anti-bait co-immunoprecipitation. The independently captured official partner record supports the protein-kinase class. This refinement characterizes the associated partner without claiming a purified interface or applying the same heterodimer composition to both cell derivatives. The original full Methods and insert sequence were unavailable. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβERBB2 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβERBB2 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official ERBB2 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβCDK1 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβCDK1 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official CDK1 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβYES1 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβYES1 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official YES1 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβHSP90AB1 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβHSP90AB1 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official HSP90AB1 record supports the Hsp90 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβTXN association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβTXN pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official TXN record supports the enzyme binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβHSPA8 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβHSPA8 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official HSPA8 record supports the Hsp70 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβCBL association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβCBL pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official CBL record supports the ubiquitin protein ligase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβYWHAQ association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβYWHAQ pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official YWHAQ record supports the 14-3-3 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | KEEP AS NON CORE | Summary: The source supports EGFRβSHC1 association within its assay context. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβSHC1 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. SHC1 is a signaling adaptor. This co-complex experiment does not independently map the EGFR contact to its SH2 or PTB domain; separate domain-binding sources are evaluated separately. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβSFN association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβSFN pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official SFN record supports the 14-3-3 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβHSPA9 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβHSPA9 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official HSPA9 record supports the Hsp70 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβSTAT3 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβSTAT3 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official STAT3 record supports the DNA-binding transcription factor binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | KEEP AS NON CORE | Summary: The source supports EGFRβGRB2 association within its assay context. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβGRB2 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. GRB2 is a signaling adaptor. The present complex-association record does not independently resolve an SH2-domain interface. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβYWHAZ association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβYWHAZ pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official YWHAZ record supports the 14-3-3 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | KEEP AS NON CORE | Summary: The source supports EGFRβCAV1 association within its assay context. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβCAV1 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. CAV1 is a caveolar membrane protein; its presence in the association does not make it an enzyme, receptor ligand or cytoskeletal protein. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβPTK2 association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβPTK2 pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official PTK2 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: The source supports EGFRβTUBA1A association with a partner-class refinement. Reason: The complete abstract describes anti-phosphotyrosine and anti-EGFR affinity purification, mass spectrometry and immunoblotting in human HN5 carcinoma cells, explicitly including direct or indirect physical associations. The exact EGFRβTUBA1A pair has a positive curated anti-bait coimmunoprecipitation record. The original body was not recovered, so detailed pair-specific assay conditions and a binary interface are not claimed. The independently checked official TUBA1A record supports the tubulin binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: tubulin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from PIK3R2. Reason: Supplementary Table 1 identifies the human PIK3R2 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to PIK3R2-N, PIK3R2-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from IRS4. Reason: Supplementary Table 1 identifies the human IRS4 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to IRS4. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from APBB3. Reason: Supplementary Table 1 identifies the human APBB3 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to APBB3-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from ABL1. Reason: Supplementary Table 1 identifies the human ABL1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to ABL1. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from NCK1. Reason: Supplementary Table 1 identifies the human NCK1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to NCK1. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from PLCG2. Reason: Supplementary Table 1 identifies the human PLCG2 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to PLCG2-N, PLCG2-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from PLCG1. Reason: Supplementary Table 1 identifies the human PLCG1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to PLCG1-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from RASA1. Reason: Supplementary Table 1 identifies the human RASA1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to RASA1-N, RASA1-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from PIK3R1. Reason: Supplementary Table 1 identifies the human PIK3R1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to PIK3R1-N, PIK3R1-C, PIK3R1-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from SHC1. Reason: Supplementary Table 1 identifies the human SHC1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to SHC1-PTB. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from ABL2. Reason: Supplementary Table 1 identifies the human ABL2 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to ABL2. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from ZAP70. Reason: Supplementary Table 1 identifies the human ZAP70 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to ZAP70-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from SYK. Reason: Supplementary Table 1 identifies the human SYK domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to SYK-C, SYK-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from CRK. Reason: Supplementary Table 1 identifies the human CRK domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to CRK. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from NUMB. Reason: Supplementary Table 1 identifies the human NUMB domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to NUMB. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from BLK. Reason: Supplementary Table 1 identifies the human BLK domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to BLK. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from GRB2. Reason: Supplementary Table 1 identifies the human GRB2 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to GRB2. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | UNDECIDED | Summary: The imported SHC2 partner cannot yet be reconciled to the study domain inventory. Reason: The imported partner is human SHC2 (P98077; current Entrez 25759). Supplementary Table 1 instead identifies the assayed SHC3 domain as Entrez 53358, and Table 4a reports an SHC3 domain measurement. The available domain inventory and measurements do not resolve the imported SHC2 pair. The original assertion is preserved pending a construct sequence or curator-level mapping that reconciles these identities; neither a wrong-gene conclusion nor a specific SHC2 domain-binding refinement is established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from PTPN11. Reason: Supplementary Table 1 identifies the human PTPN11 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to PTPN11-N. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from SLA. Reason: Supplementary Table 1 identifies the human SLA domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to SLA. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from MAPK8IP2. Reason: Supplementary Table 1 identifies the human MAPK8IP2 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to MAPK8IP2. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from PTK6. Reason: Supplementary Table 1 identifies the human PTK6 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to PTK6. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. The numeric binding measurement is for an unphosphorylated Y998 peptide; the refinement therefore does not assert phosphotyrosine dependence for this pair. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from DOK6. Reason: Supplementary Table 1 identifies the human DOK6 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to DOK5L. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from CLNK. Reason: Supplementary Table 1 identifies the human CLNK domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to MIST. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from TNS4. Reason: Supplementary Table 1 identifies the human TNS4 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to CTEN. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from PIK3R3. Reason: Supplementary Table 1 identifies the human PIK3R3 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to PIK3R3-N, PIK3R3-C, PIK3R3-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from ANKS1A. Reason: Supplementary Table 1 identifies the human ANKS1A domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to ANKS1. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from APBB2. Reason: Supplementary Table 1 identifies the human APBB2 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to APBB2-N, APBB2-C, APBB2-NC. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from SH2B1. Reason: Supplementary Table 1 identifies the human SH2B1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to SH2B. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. The numeric binding measurement is for an unphosphorylated Y998 peptide; the refinement therefore does not assert phosphotyrosine dependence for this pair. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from CISH. Reason: Supplementary Table 1 identifies the human CISH domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to CISH. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from APPL1. Reason: Supplementary Table 1 identifies the human APPL1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to APPL. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from MAPK8IP1. Reason: Supplementary Table 1 identifies the human MAPK8IP1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to MAPK8IP1. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated SH2 domain preparation from SH2B3. Reason: Supplementary Table 1 identifies the human SH2B3 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to LNK. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports SH2 domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from TLN1. Reason: Supplementary Table 1 identifies the human TLN1 domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to TLN1. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | MODIFY | Summary: EGFR-derived peptides bind the isolated PTB domain preparation from NUMBL. Reason: Supplementary Table 1 identifies the human NUMBL domain construct(s) by Entrez gene identifier, and Table 4a reports binding of the EGFR-derived peptide panel to NUMBL. The supplementary Methods describe sequence-verified human domain inserts expressed in bacteria, purified domain arrays, and concentration-dependent binding measurements. This directly supports PTB domain binding. The tested reagents are EGFR-derived peptides and isolated partner domains; the result does not itself establish a full-length native complex or transfer the partner protein's other molecular activities to EGFR. Proposed replacements: PTB domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16799092 Dynamic profiling of the post-translational modifications an... | MODIFY | Summary: The source supports EGFRβLYN association with a supported partner-class refinement. Reason: The complete source abstract reports EGFR immunoprecipitation from human A431 cells at multiple times after EGF stimulation and identification of associated proteins by mass spectrometry. The literal LYN pair is positively curated from the source with the original table/figure locators; time-dependent recovery is not interpreted as a mapped binary interface. The full original body was not recovered, so no additional pair-specific controls are claimed. LYN is a catalytically active nonreceptor protein tyrosine kinase. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16799092 Dynamic profiling of the post-translational modifications an... | MODIFY | Summary: The source supports EGFRβSFN association with a supported partner-class refinement. Reason: The complete source abstract reports EGFR immunoprecipitation from human A431 cells at multiple times after EGF stimulation and identification of associated proteins by mass spectrometry. The literal SFN pair is positively curated from the source with the original table/figure locators; time-dependent recovery is not interpreted as a mapped binary interface. The full original body was not recovered, so no additional pair-specific controls are claimed. SFN is a 14-3-3-family protein. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16799092 Dynamic profiling of the post-translational modifications an... | KEEP AS NON CORE | Summary: The source supports EGFRβCAV2 association within the measured context. Reason: The complete source abstract reports EGFR immunoprecipitation from human A431 cells at multiple times after EGF stimulation and identification of associated proteins by mass spectrometry. The literal CAV2 pair is positively curated from the source with the original table/figure locators; time-dependent recovery is not interpreted as a mapped binary interface. The full original body was not recovered, so no additional pair-specific controls are claimed. CAV2 is a caveolar scaffold/accessory protein; these data do not establish an informative narrower enzyme or cytoskeletal partner class. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16799092 Dynamic profiling of the post-translational modifications an... | KEEP AS NON CORE | Summary: The source supports EGFRβGRB2 association within the measured context. Reason: The complete source abstract reports EGFR immunoprecipitation from human A431 cells at multiple times after EGF stimulation and identification of associated proteins by mass spectrometry. The literal GRB2 pair is positively curated from the source with the original table/figure locators; time-dependent recovery is not interpreted as a mapped binary interface. The full original body was not recovered, so no additional pair-specific controls are claimed. GRB2 is a signaling adaptor. This co-purification does not map a specific SH2-domain contact. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16799092 Dynamic profiling of the post-translational modifications an... | KEEP AS NON CORE | Summary: The source supports EGFRβCAV1 association within the measured context. Reason: The complete source abstract reports EGFR immunoprecipitation from human A431 cells at multiple times after EGF stimulation and identification of associated proteins by mass spectrometry. The literal CAV1 pair is positively curated from the source with the original table/figure locators; time-dependent recovery is not interpreted as a mapped binary interface. The full original body was not recovered, so no additional pair-specific controls are claimed. CAV1 is a caveolar membrane protein. Its scaffold role does not by itself establish a narrower catalytic or cytoskeletal partner class. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17148612 A system for quantifying dynamic protein interactions define... | UNDECIDED | Summary: The imported EGFRβERBB3 assertion is unresolved for this source. Reason: The original Results explicitly report no significant EGFRβERBB3 interaction in the extracellular/transmembrane complementation system, while EGFRβERBB2 and ERBB2βERBB3 controls are positive. This construct-specific result does not refute full-length EGFRβERBB3 association established elsewhere. The positive imported pair therefore remains unresolved rather than being accepted from the paper title or interpreted as a universal negative. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17284441 Epidermal growth factor directs sex-specific steroid signali... | MODIFY | Summary: EGFR associates with the non-receptor tyrosine kinase SRC during estrogen signaling. Reason: The original Figure4 and Results show EGFR in anti-SRC immunoprecipitates from stimulated MCF-7 cells. This physical association is distinct from the fluorescent SRC-activity reporter and from downstream proliferation measurements. The verified SRC tyrosine-kinase class supports the binding refinement, without claiming a purified binary interface or transferring SRC activity to EGFR. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19167335 Large-scale structural analysis of the classical human prote... | MODIFY | Summary: An EGFR phosphopeptide is recognized by the protein phosphatase PTPRB. Reason: The imported P23467 identifier maps to PTPRB, not PTPN9. The literal interaction record identifies a PTPRB1686β1971 catalytic-domain preparation acting on EGFR1066β1076 phosphorylated at1069, consistent with the original comparative phosphatase assay. The refinement preserves this peptide-based substrate-recognition scope and does not claim a native full-length receptor complex. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβANXA1 association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβANXA1 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. ANXA1 is a calcium/phospholipid-binding regulatory protein; the verified association does not assign its calcium-binding activity to EGFR. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβGAPDH binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβGAPDH record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3C, figure legend:Table S6. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. The independently checked official GAPDH classification supports enzyme binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβHSP90AA1 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβHSP90AA1 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official HSP90AA1 classification supports Hsp90 protein binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβHSP90AB1 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβHSP90AB1 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official HSP90AB1 classification supports Hsp90 protein binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβUCHL1 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβUCHL1 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3C, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. UCHL1 is a ubiquitin C-terminal hydrolase/peptidase. Its disputed ubiquitin-ligase activity is not used to classify this pair. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβTXN binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβTXN record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official TXN classification supports enzyme binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβGOT1 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβGOT1 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official GOT1 classification supports enzyme binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβCFL1 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβCFL1 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official CFL1 classification supports cytoskeletal regulatory protein binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβYWHAQ binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβYWHAQ record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0006"(anti bait coimmunoprecipitation), psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3A, figure legend:S3C, figure legend:Table S6. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. The independently checked official YWHAQ classification supports 14-3-3 protein binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβSTIP1 association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβSTIP1 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3C, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. STIP1 is an HSP70βHSP90 co-chaperone. The saved official evidence does not resolve its own nascent/unfolded-client binding sufficiently for GO:0051087. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβHSPA4 association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβHSPA4 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The saved HSPA4 record identifies a heat-shock protein but lacks a FUNCTION account establishing the more specific client-handling class. The binding observation is retained while this class remains unresolved. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβHSPA9 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβHSPA9 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official HSPA9 classification supports Hsp70 protein binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβGABARAPL2 association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβGABARAPL2 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0096"(pull down), with locators figure legend:S3B, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. GABARAPL2 is an autophagy-related ubiquitin-like modifier, not the conjugating enzyme that acts on it. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβAKAP12 association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβAKAP12 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3C, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. AKAP12 is a kinase-anchoring scaffold; it is not the protein kinase recruited by that scaffold. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβPTPN12 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβPTPN12 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official PTPN12 classification supports protein phosphatase binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβAHNAK association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβAHNAK record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The available AHNAK evidence does not establish an informative narrower partner class for this association. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβMAP3K12 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβMAP3K12 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0006"(anti bait coimmunoprecipitation), with locators figure legend:Fig 1C|agonist:"\"EGF (Species unknown)\"", figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. The independently checked official MAP3K12 classification supports protein kinase binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβFKBP8 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβFKBP8 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0006"(anti bait coimmunoprecipitation), psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3A, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. FKBP8 has documented peptidyl-prolyl isomerase activity conditional on calcium/calmodulin; enzyme-class binding does not assert that the activity occurred in this interaction assay. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβAP2M1 association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβAP2M1 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. AP2M1 is an adaptor-complex cargo-recognition subunit; this source does not establish a narrower domain-binding interface for the imported assertion. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | KEEP AS NON CORE | Summary: The source supports EGFRβVAPA association with bounded assay scope. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβVAPA record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3C, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. VAPA is a membrane-contact-site/vesicle-associated protein, not a SNARE classified from its name. The positive protein association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβHDAC6 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβHDAC6 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0006"(anti bait coimmunoprecipitation), psi-mi:"MI:0007"(anti tag coimmunoprecipitation), psi-mi:"MI:0424"(protein kinase assay), with locators figure legend:Fig 1C|agonist:"\"EGF (Species unknown)\"", figure legend:Fig 2, figure legend:Fig 2c, figure legend:Fig 5F, figure legend:Fig S4C|agonist:"\"EGF (Species unknown)\"", figure legend:S4A, figure legend:S4D, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. The source maps EGFR645β672 and HDAC61010β1050 in the interaction assay and separately reports a kinase assay with EGFR712β979; these fragments are not natural-product identities. HDAC6 is an enzyme with documented deacetylase activity; its nonhistone substrate scope does not justify inferring a histone-specific interaction from its name. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβSTUB1 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβSTUB1 record is linked to the MYTH screen. No native complex or physiological encounter is inferred from this binary screen alone. The independently checked official STUB1 classification supports ubiquitin protein ligase binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20029029 Regulation of epidermal growth factor receptor trafficking b... | MODIFY | Summary: The source supports EGFRβMAST1 binding with an informative partner-class refinement. Reason: The original study used a split-ubiquitin MYTH screen with human EGFR residues25β1210 and a yeast secretion signal; it reports that EGFR was not tyrosine-phosphorylated in this yeast system. The literal positive EGFRβMAST1 record is linked to the MYTH screen. The curated source records additionally report psi-mi:"MI:0007"(anti tag coimmunoprecipitation), with locators figure legend:S3C, figure legend:Table S1. These method/figure assignments are retained as curated source metadata; the supplementary figure pixels were not independently inspected. The independently checked official MAST1 classification supports protein kinase binding. The refinement identifies the verified binding partner class and does not transfer its catalytic activity to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | MODIFY | Summary: FAK association supports protein tyrosine kinase binding. Reason: Reciprocal FAK/EGFR precipitation supports the association. Official Q05397 identifies FAK as a protein tyrosine kinase; the affected expression-of-concern panel is distinct. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | MODIFY | Summary: SHP2 association supports protein phosphatase binding. Reason: The positive SHP2 association and official Q06124 phosphatase class support the refinement; no direct binary contact is required or claimed. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20473329 SIRPalpha1 receptors interfere with the EGFRvIII signalosome... | KEEP AS NON CORE | Summary: Retain the positive SOS1 association as contextual binding. Reason: SOS1 is a guanine-nucleotide exchange factor. The bounded term search found no fitting GEF-binding term; exchange-factor function alone does not justify enzyme binding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20624308 EGFR/Met association regulates EGFR TKI resistance in breast... | MODIFY | Summary: SRC association supports protein tyrosine kinase binding. Reason: The positive SUM229 association and human SRC kinase class support this refinement, with the distinct SUM149 result retained. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20878056 Critical involvement of RQCD1 in the EGFR-Akt pathway in mam... | KEEP AS NON CORE | Summary: The EGFR intracellular fragment binds RQCD1/CNOT9 in the reported assay. Reason: The original Methods identify the human EGFR His676βAla1210 fragment and GST-RQCD1/CNOT9. Affinity-purified EGFR fragment is recovered by GST-RQCD1 in the separate binding assay, providing evidence beyond cellular co-complex recovery. The official CNOT9 record describes a noncatalytic CCR4-NOT component; its association with a deadenylase complex does not make it a catalytic enzyme partner. The supported generic binding is retained without inventing a more specific partner class. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20935677 A positive feedback loop of ER-Ξ±36/EGFR promotes malignant g... | MODIFY | Summary: The SRC-containing complex supports protein tyrosine kinase binding. Reason: The positive complex association and independent human SRC kinase class support the refinement without a purified-interface claim. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20935677 A positive feedback loop of ER-Ξ±36/EGFR promotes malignant g... | MODIFY | Summary: SHC1 association supports binding to a signaling scaffold. Reason: Independent official SHC1 evidence describes receptor-to-GRB2/SOS tethering. Preserve product-dependent functional limits; the paper does not authenticate the detected Shc product or an SH2 interface. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | UNDECIDED | Summary: The source-specific ERBB3 association remains unresolved. Reason: The limited negative detection result in one low-EGFR context cannot adjudicate every imported positive assay. The relevant supplemental evidence remains inaccessible. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21278786 PI3K inhibition results in enhanced HER signaling and acquir... | UNDECIDED | Summary: The source-specific GRB2 association requires the unavailable supplement. Reason: Failure to observe increased association does not show absence of basal association. Retain uncertainty until the relevant supplemental assay is inspectable. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21278788 Translationally controlled tumor protein induces human breas... | UNDECIDED | Summary: The SHC1 pair remains unverified at source-assay resolution. Reason: The abstract does not resolve the SHC1 association; operative pair Methods and Results were not recovered. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21278788 Translationally controlled tumor protein induces human breas... | UNDECIDED | Summary: The GRB2 pair remains unverified at source-assay resolution. Reason: The abstract does not resolve the GRB2 association; operative pair Methods and Results were not recovered. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21278788 Translationally controlled tumor protein induces human breas... | UNDECIDED | Summary: The GAB1 pair remains unverified at source-assay resolution. Reason: The abstract does not resolve the GAB1 association; operative pair Methods and Results were not recovered. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | KEEP AS NON CORE | Summary: Retain the measured EGFRβANKRD13B association with its ubiquitin-dependent mechanism. Reason: The study reports EGF-dependent association of ubiquitinated EGFR with transfected ANKRD13A/B/D in human HeLa cells. The endogenous ANKRD13B signal was not detected under the reported antibody/expression conditions; the positive transfected-protein result remains distinct. The ANKRD13 UIMs recognize the ubiquitin moiety on EGFR, and a stripped-receptor assay separates this from associated cellular proteins. These findings support the imported protein-association assertion but do not establish binding to an ankyrin repeat or give EGFR ubiquitin-binding activity. No informative partner-class refinement is established by the saved class records, so the supported generic term is retained under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22298428 The Ankrd 13 family of UIM-bearing proteins regulates EGF re... | KEEP AS NON CORE | Summary: Retain the measured EGFRβANKRD13A association with its ubiquitin-dependent mechanism. Reason: The study reports EGF-dependent association of ubiquitinated EGFR with transfected ANKRD13A/B/D in human HeLa cells. Endogenous ANKRD13A/D association was also detected. The ANKRD13 UIMs recognize the ubiquitin moiety on EGFR, and a stripped-receptor assay separates this from associated cellular proteins. These findings support the imported protein-association assertion but do not establish binding to an ankyrin repeat or give EGFR ubiquitin-binding activity. No informative partner-class refinement is established by the saved class records, so the supported generic term is retained under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22439932 NKX2-1/TITF1/TTF-1-Induced ROR1 is required to sustain EGFR ... | MODIFY | Summary: EGFR associates with the signaling receptor ROR1. Reason: Literal curated records identify human EGFRβROR1 co-immunoprecipitation and construct features, while the available abstract supports a kinase-independent receptor-complex role. Full operative Methods were not recovered. Official ROR1 evidence establishes a ligand-responsive receptor but also cautions that its kinase domain has very low activity and does not bind ATP in the cited assays. Signaling-receptor binding therefore captures the verified partner class without promoting ROR1 to an ordinary active receptor tyrosine kinase or treating the curated feature coordinates as personally read experimental methods. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23178716 SnoN/SkiL expression is modulated via arsenic trioxide-induc... | MODIFY | Summary: EGFR associates with the signaling scaffold GRB2 in HEY cells. Reason: The original directly measures GRB2 recovery in EGFR and SHC-associated immunoprecipitates after EGF or arsenic trioxide stimulation. Association kinetics and phosphorylation patterns differ between stimuli. Independent GRB2 evidence establishes tethering of receptor-associated signaling partners, supporting scaffold-protein binding without assuming a specific SH2-domain interface was mapped in this experiment. The same paper cannot resolve p46/p52ShcA bands, a limitation not transferred to the distinct GRB2 measurement. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23397142 Analysis of protein-protein interactions in cross-talk pathw... | UNDECIDED | Summary: The source establishes EGFRβCRKL proximity, with physical binding unresolved. Reason: Literal records and the original identify proximity-ligation evidence for EGFRβCRKL in liver cancer cells. The functional perturbation and orthogonal network experiments focus on other pairs, including CRKLβFLT1, and cannot substitute for a verified EGFRβCRKL binding assay. CRKL is a signaling adaptor, but partner identity alone does not convert proximity into physical binding. The positive spatial observation remains recorded without a scaffold-binding refinement. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23436906 Parallel visualization of multiple protein complexes in indi... | MODIFY | Summary: EGFR associates with ERBB3 with corroboration beyond proximity ligation. Reason: The original study visualizes receptor proximity by multiplex proximity ligation in cell systems and human breast tumor tissue. Its own discussion distinguishes proximity from direct binding and notes possible chance proximity at high abundance. The separately read EGFR TAP/co-IP study provides physical-association evidence for the exact ERBB3 partner. Together with the verified receptor class, this supports the refinement while retaining the distinct assays and mutant/tumor contexts; no purified interface is claimed. Proposed replacements: signaling receptor binding |
| GO:0005515 protein binding | IPI PMID:23764002 Epidermal growth factor receptor potentiates MCM7-mediated D... | MODIFY | Summary: EGFR associates with the explicitly indexed LYN isoform-1 partner. Reason: The imported P07948-1 identity is preserved. The original distinguishes p56 and p53 LYN and shows EGFR association with both, with preferential EGF-dependent recruitment and Y32 phosphorylation of p56. The source feature record includes the p56 N-terminal region and mutation experiments; no corresponding Y32 mechanism is asserted for p53. Non-receptor-tyrosine-kinase binding captures the assayed partner class while keeping receptor association separate from LYN-dependent MCM7 phosphorylation. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23799367 Threshold-controlled ubiquitination of the EGFR directs rece... | MODIFY | Summary: EGFR associates with the signaling scaffold SHC1 in the receptor-ubiquitination study. Reason: The original receptor immunoprecipitations directly assess SHC recruitment alongside GRB2 and CBL. Independently established SHC1 tethering of activated receptors to signaling partners supports scaffold-protein binding. The association is not used to infer a specific SH2 or PTB contact or to identify a natural SHC1 isoform from an unresolved band. SHC binding and CBL-catalyzed receptor ubiquitination are distinct steps. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23799367 Threshold-controlled ubiquitination of the EGFR directs rece... | MODIFY | Summary: EGFR associates with the signaling scaffold GRB2 during CBL recruitment. Reason: Original co-immunoprecipitation and purified recruitment experiments distinguish GRB2 association from CBL-mediated receptor ubiquitination. GRB2 links the receptor-associated signaling complex and CBL, consistent with its independently established tethering role. Scaffold-protein binding captures this partner class without making GRB2 or EGFR the E3 ligase and without requiring a purified autonomous full-length receptor complex in every assay. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | MODIFY | Summary: EGFR associates with YES1 in the tested lung-cancer cell context. Reason: The original H1975 experiments recover the EGFRβYES1 complex by coimmunoprecipitation, with an anti-vimentin control. The independently captured official partner record establishes the protein-kinase class. The refinement describes the binding partner, not transfer of its catalytic activity to EGFR. Cellular inhibitor dependencies are not substituted for a purified binary contact or direct cross-phosphorylation assay. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | MODIFY | Summary: EGFR associates with LYN in the tested lung-cancer cell context. Reason: The original Calu-3 experiments recover LYN with EGFR rather than MET; the negative FYN comparison is a separate partner result. The independently captured official partner record establishes the protein-kinase class. The refinement describes the binding partner, not transfer of its catalytic activity to EGFR. Cellular inhibitor dependencies are not substituted for a purified binary contact or direct cross-phosphorylation assay. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | MODIFY | Summary: EGFR associates with MET in the tested lung-cancer cell context. Reason: The original Calu-3 experiments recover EGFR together with MET, ERBB2 and ERBB3 by coimmunoprecipitation. The independently captured official partner record establishes the protein-kinase class. The refinement describes the binding partner, not transfer of its catalytic activity to EGFR. Cellular inhibitor dependencies are not substituted for a purified binary contact or direct cross-phosphorylation assay. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23866081 Lyn, a Src family kinase, regulates activation of epidermal ... | MODIFY | Summary: EGFR associates with ERBB3 in the tested lung-cancer cell context. Reason: The original Calu-3 experiments recover EGFR together with MET, ERBB2 and ERBB3 by coimmunoprecipitation. The independently captured official partner record establishes the receptor class. The refinement describes the binding partner, not transfer of its catalytic activity to EGFR. Cellular inhibitor dependencies are not substituted for a purified binary contact or direct cross-phosphorylation assay. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24034250 EGFR-mediated Beclin 1 phosphorylation in autophagy suppress... | KEEP AS NON CORE | Summary: The source supports an EGFR-associated RUBCN-containing complex. Reason: The literal RUBCN record is an association obtained by spoke expansion from the Figure 4I co-complex experiment. It supports a complex association, with less resolution than an isolated EGFRβRUBCN binary assay. The positive protein-binding assertion is retained with that method distinction. RUBCN-mediated regulation of the autophagy complex is not transferred as enzyme activity to either binding partner, and the unrecovered full experimental detail remains explicit. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | KEEP AS NON CORE | Summary: The source supports EGFRβANXA1 association within its assay context. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. ANXA1 binds calcium and phospholipids, but this association does not establish a more informative supported protein-partner class. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβERBB2 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source also has a pair-specific coimmunoprecipitation record; its S1B/S1C caption-label ambiguity is retained in the source projection rather than silently resolved. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official ERBB2 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβHSP90AA1 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official HSP90AA1 record supports the Hsp90 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβHSP90AB1 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official HSP90AB1 record supports the Hsp90 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβMET association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official MET record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβHSPA8 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official HSPA8 record supports the Hsp70 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβCDH1 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official CDH1 record supports the cadherin binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβERBB3 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source also has a pair-specific coimmunoprecipitation record; its S1B/S1C caption-label ambiguity is retained in the source projection rather than silently resolved. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. ERBB3 is a signaling receptor with limited kinase activity; the receptor-binding class avoids attributing its heterodimer partner's stronger catalytic activity to it. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβYWHAQ association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official YWHAQ record supports the 14-3-3 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | KEEP AS NON CORE | Summary: The source supports EGFRβSHC1 association within its assay context. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source also has a pair-specific coimmunoprecipitation record; its S1B/S1C caption-label ambiguity is retained in the source projection rather than silently resolved. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. SHC1 is a signaling adaptor. This co-complex experiment does not independently map the EGFR contact to its SH2 or PTB domain; separate domain-binding sources are evaluated separately. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβSFN association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official SFN record supports the 14-3-3 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβHSPA9 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official HSPA9 record supports the Hsp70 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβSTAT3 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source also has a pair-specific coimmunoprecipitation record; its S1B/S1C caption-label ambiguity is retained in the source projection rather than silently resolved. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official STAT3 record supports the DNA-binding transcription factor binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | KEEP AS NON CORE | Summary: The source supports EGFRβGRB2 association within its assay context. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. GRB2 is a signaling adaptor. The present complex-association record does not independently resolve an SH2-domain interface. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | KEEP AS NON CORE | Summary: The source supports EGFRβAHNAK association within its assay context. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The available AHNAK evidence does not establish a more informative narrower partner class for this association. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | KEEP AS NON CORE | Summary: The source supports EGFRβAP1B1 association within its assay context. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. AP1B1 is an adaptor-complex subunit; this complex-association result does not establish a narrower domain-binding interface. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβCDC37 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source also has a pair-specific coimmunoprecipitation record; its S1B/S1C caption-label ambiguity is retained in the source projection rather than silently resolved. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. CDC37 binds kinase clients and stabilizes an unfolded kinase intermediate in the human HSP90βCDC37βCDK4 structure (PMID:27339980). The chaperone partner class does not require EGFR itself to perform protein folding. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein-folding chaperone binding |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβTUBA1A association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official TUBA1A record supports the tubulin binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: tubulin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | KEEP AS NON CORE | Summary: The source supports EGFRβAP2M1 association within its assay context. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. AP2M1 is an adaptor-complex cargo-recognition subunit; this source does not map a narrower binding interface. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | KEEP AS NON CORE | Summary: The source supports EGFRβERRFI1 association within its assay context. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source also has a pair-specific coimmunoprecipitation record; its S1B/S1C caption-label ambiguity is retained in the source projection rather than silently resolved. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. ERRFI1 is a receptor-associated inhibitor; inhibition of a kinase is distinct from possessing kinase activity. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The source supports EGFRβBAIAP2 association with a partner-class refinement. Reason: The original study maps affinity-purified human EGFR complexes in lung-cell models, including wild-type receptor and the activating exon-19 deletion E746βA750. The exact pair is present in the curated TAP records; construct features, bait direction and any follow-up coimmunoprecipitation are preserved separately. Co-purification supports physical association without establishing a purified binary interface. The source network discarded isoform distinctions, so no natural-product-specific equivalence is inferred. The independently checked official BAIAP2 record supports the cytoskeletal regulatory protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PIK3C2B association supports phosphatidylinositol 3-kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row7 PIK3C2B (WT/background 1,22; L858R/background 4,31). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PIK3C2B is a phosphatidylinositol 3-kinase with documented lipid phosphorylation, rather than a protein kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: phosphatidylinositol 3-kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported LAT association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row105 LAT (WT/background 29,54; L858R/background 18,37). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. LAT is a signaling adaptor. The association supports binding, but does not assign its adaptor function to EGFR or map a more informative binding interface in this source. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured TLR2 association supports signaling receptor binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row9 TLR2 (WT/background 0,59; L858R/background 1,69). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. TLR2 is a signaling receptor; receptor-binding does not itself assert agonism or transfer TLR2 signaling activity to EGFR. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured CTNND1 association supports cytoskeletal regulatory protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row68 CTNND1 (WT/background 3,00; L858R/background 3,63). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CTNND1 regulates Rho-family GTPases and downstream cytoskeletal dynamics; the selected class concerns binding to that regulatory protein. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported GRAP2 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row4 GRAP2 (WT/background 1,79; L858R/background 8,11). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. GRAP2 is an SH2/SH3 adaptor; possession of these domains alone does not show which domain the full-protein MaMTH association engages. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured ABL1 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row123 ABL1 (WT/background 1,88; L858R/background 0,49). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. ABL1 is a catalytically active non-receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured TGFA association supports growth factor binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row104 TGFA (WT/background 2,52; L858R/background 1,59). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. TGFA is an EGFR growth-factor ligand; this is growth-factor binding, without renaming TGFA as EGF. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured RAF1 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row98 RAF1 (WT/background 4,91; L858R/background 3,81). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. RAF1 is a serine/threonine protein kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured NR3C1 association supports nuclear receptor binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row95 NR3C1 (WT/background 3,21; L858R/background 2,58). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. NR3C1 is a glucocorticoid-regulated nuclear receptor; binding to this partner does not establish that EGFR itself binds a DNA regulatory sequence. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: nuclear receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured GAPDH association supports enzyme binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row78 GAPDH (WT/background 3,43; L858R/background 3,80). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. GAPDH is a glyceraldehyde-3-phosphate dehydrogenase. The informative supported category is enzyme binding, without assigning its metabolic chemistry to EGFR. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured CDK1 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row69 CDK1 (WT/background 1,64; L858R/background 1,97). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CDK1 is a cyclin-dependent protein kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured HSP90AA1 association supports Hsp90 protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row62 Hsp90AA1 (WT/background 74,23; L858R/background 97,06). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. HSP90AA1 is an Hsp90-family chaperone. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured LYN association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row56 LYN (WT/background 6,92; L858R/background 9,74). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. LYN is a non-receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured HSP90AB1 association supports Hsp90 protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row111 HSP90AB1 (WT/background 27,59; L858R/background 14,76). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. HSP90AB1 is an Hsp90-family chaperone. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured HCK association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row85 HCK (WT/background 3,93; L858R/background 3,96). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. HCK is a non-receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured FGR association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row119 FGR (WT/background 4,64; L858R/background 1,93). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. FGR is a non-receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured TXN association supports enzyme binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row59 TXN (WT/background 5,09; L858R/background 7,04). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. TXN catalyzes dithiol-disulfide exchange; enzyme binding describes the partner class without assigning redox catalysis to EGFR. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured HSPA8 association supports Hsp70 protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row45 HSPA8 (WT/background 24,99; L858R/background 40,87). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. HSPA8 is the Hsp70-family cognate chaperone with documented folding and transport of nascent polypeptides. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured CDH1 association supports cadherin binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row82 CDH1 (WT/background 2,14; L858R/background 2,27). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CDH1 is E-cadherin, a type I membrane cell-adhesion protein. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured SRC association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row73 SRC (WT/background 11,15; L858R/background 12,89). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. SRC is a non-receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported JUP association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row13 JUP (WT/background 0,97; L858R/background 2,50). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. JUP is a junctional plaque protein. The measured association is retained without equating every plaque component with an actin, microtubule or intermediate-filament constituent. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured EZR association supports cytoskeletal protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row108 EZR (WT/background 8,28; L858R/background 5,00). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. EZR links cytoskeletal structures to the plasma membrane and is a cortical cytoskeletal protein. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported MUC1 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row5 MUC1 (WT/background 1,08; L858R/background 4,20). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. MUC1 is a membrane mucin with distinct extracellular and intracellular functions; this whole-protein association does not identify a supported narrower EGFR binding activity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PDGFRA association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row51 PDGFRA (WT/background 9,16; L858R/background 13,73). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PDGFRA is a receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported NCK1 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row87 NCK1 (WT/background 2,20; L858R/background 2,15). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. NCK1 is a signaling adaptor; the source does not localize the measured association to its SH2 or SH3 domains. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PLCG2 association supports phospholipase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row107 PLCG2 (WT/background 3,98; L858R/background 2,43). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PLCG2 is a phospholipase C that hydrolyzes phosphatidylinositol bisphosphate. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: phospholipase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PRKCA association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row101 PRKCA (WT/background 11,12; L858R/background 7,65). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PRKCA is a serine/threonine protein kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PTPN1 association supports protein phosphatase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row66 PTPN1 (WT/background 44,56; L858R/background 55,89). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PTPN1 is a protein tyrosine phosphatase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured CFL1 association supports cytoskeletal regulatory protein binding. Reason: Supplementary Figure3d directly shows the EGFR-CFL1 positive control in the mLexA-VP16 MaMTH reporter, above the bait-only control; the curated record also points to Figure1c. This control is outside the 205-prey/124-positive screening tables. CFL1 binds and depolymerizes actin filaments and is a regulator of cytoskeletal reorganization. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported S100A4 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row12 S100A4 (WT/background 1,72; L858R/background 4,46). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. S100A4 is a calcium-binding regulatory protein; binding to S100A4 is not evidence that EGFR binds calcium or a calcium channel. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured YWHAQ association supports 14-3-3 protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row53 YWHAQ (WT/background 8,19; L858R/background 11,94). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. YWHAQ is a 14-3-3-family protein. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported SHC1 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row47 SHC1 (WT/background 11,47; L858R/background 17,93). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. The imported SHC1 isoform identifier is retained. The curated record includes the positive-control and mutant contexts; a reference-sequence identifier is not independent verification of every experimental insert or natural-product equivalence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured AKT1 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row99 AKT1 (WT/background 4,41; L858R/background 3,11). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. AKT1 is a serine/threonine protein kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured SFN association supports 14-3-3 protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row11 SFN (WT/background 5,60; L858R/background 14,70). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. SFN is the 14-3-3 sigma protein. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured ARRB2 association supports arrestin family protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row27 ARRB2 (WT/background 2,52; L858R/background 5,38). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. ARRB2 is a beta-arrestin family member. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: arrestin family protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported HSPA4 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row25 HSPA4 is identified as a heat-shock protein in the official record, but the saved record lacks a FUNCTION account establishing the specific nascent/unfolded-client-handling property needed for a chaperone-class refinement. The positive pair is retained as non-core under the project policy. This uncertainty concerns the partner classification, not a requirement to demonstrate that EGFR is a folding client or to map a purified interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured STAT3 association supports DNA-binding transcription factor binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row110 STAT3 (WT/background 7,35; L858R/background 4,19). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. STAT3 is a sequence-specific DNA-binding transcription factor; partner-class binding does not imply a nuclear EGFR-STAT3 transcriptional complex in this assay. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured STAT1 association supports DNA-binding transcription factor binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row52 STAT1 (WT/background 4,65; L858R/background 6,80). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. STAT1 binds defined response elements and activates transcription; this refinement identifies its partner class. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured STAT5A association supports DNA-binding transcription factor binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row83 STAT5A (WT/background 3,12; L858R/background 3,26). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. STAT5A binds the GAS DNA element and activates transcription; this refinement identifies its partner class. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured ABL2 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row88 ABL2 (WT/background 4,63; L858R/background 4,46). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. ABL2 is a non-receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured ZAP70 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row89 ZAP70 (WT/background 16,91; L858R/background 16,24). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. ZAP70 is a protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported CRK association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row21 CRK (WT/background 4,01; L858R/background 9,35). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CRK is an adaptor, not a kinase. Table4 labels CRK and CRKII separately; the literal curated record maps this assertion to Table4 row21, without independently authenticating the insert sequence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported CRK association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row41 CRKII (WT/background 7,29; L858R/background 12,62). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. The imported CRK isoform identifier is preserved. The curated record maps its screen result to Table4 row41 (CRKII) and also records LUMIER and mutational assays; no equivalence of all natural CRK products is inferred. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported CRKL association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row61 CRKL (WT/background 10,30; L858R/background 13,66). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CRKL is an SH2/SH3 adaptor; the full-protein association does not itself map an SH2-binding interface or establish kinase catalysis. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported CAMLG association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row86 CAMLG (WT/background 7,16; L858R/background 7,16). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CAMLG participates in the tail-anchored protein insertion machinery. Its association does not establish that EGFR carries out that insertion activity or binds an ion channel. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured ARRB1 association supports arrestin family protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row17 ARRB1 (WT/background 2,72; L858R/background 6,57). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. ARRB1 is a beta-arrestin family member. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: arrestin family protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured BLK association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row39 BLK (WT/background 4,53; L858R/background 8,25). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. BLK is a protein tyrosine kinase; its catalytic classification has direct human literature provenance in the official record. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported CAV2 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row14 CAV2 (WT/background 2,57; L858R/background 6,57). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CAV2 is a caveolar scaffold; the association is retained without assigning caveolar assembly or another partner activity to EGFR. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported GRB2 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row8 GRB2 (WT/background 10,03; L858R/background 35,37). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. GRB2 is a non-enzymatic signaling adaptor. This source's whole-protein interaction is retained without treating adaptor recruitment alone as a new catalytic or DNA-binding activity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured YWHAZ association supports 14-3-3 protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row36 YWHAZ (WT/background 7,58; L858R/background 13,94). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. YWHAZ is a 14-3-3-family protein. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported CAV1 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row74 CAV1 (WT/background 1,86; L858R/background 2,14). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CAV1 is a caveolar scaffold; association is supported without equating caveolin with a catalytic enzyme or an integral cytoskeletal polymer. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PTPN12 association supports protein phosphatase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row115 PTPN12 (WT/background 2,65; L858R/background 1,22). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PTPN12 is a protein tyrosine phosphatase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PTK2 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row60 PTK2 (WT/background 4,07; L858R/background 5,59). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PTK2 is a non-receptor protein tyrosine kinase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured EPS8 association supports cytoskeletal regulatory protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row28 EPS8 (WT/background 2,62; L858R/background 5,57). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. EPS8 directly regulates actin-filament capping and bundling, supporting the cytoskeletal regulatory partner class. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured TRAF2 association supports ubiquitin protein ligase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row114 TRAF2 (WT/background 7,50; L858R/background 3,47). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. TRAF2 has a documented E3 ubiquitin-ligase reaction; binding does not establish EGFR ubiquitin-ligase activity. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. The TRAF2 ubiquitin-ligase classification is supported by its explicit official catalytic annotation and a recombinant-protein experiment, not merely its name or recruitment of cIAP ligases. PMID:20577214 reports S1P-dependent TRAF2-mediated RIP1 ubiquitination with E1/E2, RING-deletion and linkage controls, and separately excludes cIAP1/2 and TRAF5 from the tested preparation. Thus GO:0031625 describes binding to a partner with demonstrated conditional E3 activity. It does not assign ubiquitination to EGFR or claim that TRAF2 acts catalytically in this interaction assay; TRAF2 also has distinct cIAP-recruitment roles. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported LCP2 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row22 LCP2 (WT/background 2,71; L858R/background 6,28). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. LCP2 is an adaptor; its SH2 domain and signaling role do not by themselves locate the interface measured in this assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported SLA association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row118 SLA (WT/background 2,78; L858R/background 1,19). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. SLA is a Src-like adaptor rather than a Src-family catalytic kinase. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported GRB10 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row77 GRB10 (WT/background 3,14; L858R/background 3,49). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. GRB10 is an adaptor. Its SH2 domain is present, but this full-protein assay does not independently establish a domain-specific interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported MAPK8IP2 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row81 MAPK8IP2 (WT/background 1,52; L858R/background 1,63). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. MAPK8IP2 is a JNK pathway scaffold rather than a MAP kinase; the association does not transfer kinase activity to either binding partner. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported GAB1 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row16 GAB1 (WT/background 0,93; L858R/background 2,31). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. GAB1 is a signaling adaptor rather than an enzyme or DNA-binding transcription factor. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured CTTN association supports cytoskeletal regulatory protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row103 CTTN (WT/background 33,81; L858R/background 22,11). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CTTN regulates cortical actin organization and cell shape. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported TAB1 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row84 TAB1 (WT/background 5,85; L858R/background 5,94). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. TAB1 is a kinase-associated adaptor, not itself a demonstrated protein kinase in this record. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured NTRK2 association supports protein kinase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row106 NTRK2 (WT/background 1,56; L858R/background 0,96). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. NTRK2 is a receptor protein tyrosine kinase. The generic accession-level result is not extended to every natural truncated NTRK2 product. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured TNS3 association supports cytoskeletal regulatory protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row23 TNS3 (WT/background 1,40; L858R/background 3,12). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. TNS3 regulates integrin-actin coupling and Rho-family-dependent cytoskeletal organization. Its only probable phosphatase activity is not used to select a phosphatase-binding class. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported SHC4 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row26 SHC4 (WT/background 5,32; L858R/background 11,39). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. SHC4 is a signaling adaptor. The whole-protein assay does not identify a particular SH2/PTB interface or a catalytic activity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured TUBA1A association supports tubulin binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row19 TUBA1A (WT/background 1,13; L858R/background 2,67). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. TUBA1A is an alpha-tubulin constituent of microtubules. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: tubulin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured HDAC7 association supports histone deacetylase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row38 HDAC7 (WT/background 2,37; L858R/background 4,34). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. HDAC7 is a class II histone deacetylase/corepressor. The classification uses the official functional annotation, including its similarity-based histone-substrate scope, rather than transferring deacetylase catalysis to EGFR. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: histone deacetylase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PIK3R3 association supports phosphatidylinositol 3-kinase regulatory subunit binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row48 PIK3R3 (WT/background 1,55; L858R/background 2,40). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PIK3R3 is the regulatory gamma subunit of PI3K, rather than its catalytic subunit. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported ANKS1A association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row63 ANKS1A (WT/background 9,27; L858R/background 11,75). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. ANKS1A is a signaling regulator/adaptor; its association is retained without inventing a domain-binding or enzymatic class. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported APBB2 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row90 APBB2 (WT/background 3,05; L858R/background 2,91). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. APBB2 is an adaptor with several interaction domains; this assay does not map a specific interface that would support a narrower binding term. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported SH2D3A association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row50 SH2D3A (WT/background 4,75; L858R/background 7,23). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. SH2D3A is an SH2-containing signaling protein; domain presence alone does not identify the interface of the full-protein association. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported SH2B1 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row65 SH2B1 (WT/background 2,98; L858R/background 3,76). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. SH2B1 is a receptor-associated adaptor; this whole-protein assay does not resolve which of its domains mediates binding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported CISH association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row29 CISH (WT/background 1,29; L858R/background 2,67). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. CISH is a SOCS-family regulatory protein; the association does not establish that CISH is itself a catalytic ubiquitin ligase or that EGFR recognizes an SH2-domain interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the reported ITSN2 association as non-core binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row122 ITSN2 (WT/background 2,10; L858R/background 0,62). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. ITSN2 is a multidomain endocytic adaptor with isoform-dependent signaling domains. The current whole-protein source does not establish a specific catalytic partner class for the imported accession. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured HDAC6 association supports enzyme binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row109 HDAC6 (WT/background 24,86; L858R/background 14,82). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. HDAC6 is a protein deacetylase with well-established non-histone substrates. The current official caution distinguishes this from its historical histone-deacetylase designation, so the supported refinement is enzyme binding. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured STUB1 association supports ubiquitin protein ligase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row102 STUB1 (WT/background 10,28; L858R/background 7,06). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. STUB1 is an E3 ubiquitin-protein ligase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured WASF3 association supports cytoskeletal regulatory protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row44 WASF3 (WT/background 1,30; L858R/background 2,14). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. WASF3 regulates cytoskeletal organization and actin-dependent cell morphology. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured BAIAP2 association supports cytoskeletal regulatory protein binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row49 BAIAP2 (WT/background 4,83; L858R/background 7,37). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. BAIAP2 regulates CDC42/RAC1-dependent actin reorganization and actin bundling. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The measured PTPN22 association supports protein phosphatase binding. Reason: The source reports a MaMTH association in human HEK293T reporter cells: Table4 row124 PTPN22 (WT/background 2,99; L858R/background 0,39). Table4 calls positives for WT and/or L858R; these ratios are not an independent significance calculation and do not establish an equivalent endogenous complex. PTPN22 is a protein tyrosine phosphatase. This is a partner-class binding assertion, not a transfer of the partner's activity or proof that EGFR is its physiological substrate. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | MODIFY | Summary: EGFR associates with the kinase-client chaperone CDC37. Reason: The exact source-linked LUMIER records include wild-type and engineered EGFR preparations; they retain the exon-deletion and mutation features separately. The main original describes physical capture in 293T cells and demonstrates the kinase-client preference of CDC37. Independent human structural evidence shows CDC37 engaging an unfolded kinase client (PMID:27339980). This supports protein-folding chaperone binding without requiring EGFR itself to perform folding or treating every mutant as the canonical receptor. Proposed replacements: protein-folding chaperone binding |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | MODIFY | Summary: The reported Hsp70 association supports chaperone-partner binding. Reason: The source explicitly measures Hsp70 interactions by the physical-capture LUMIER assay, and the literal EGFR pair records are positive with their receptor mutations and treatment contexts retained. The paper identifies the partner as a chaperone; the class refinement does not depend on an assumed purified interface. The current Q53FC7 reference is 643 residues and retains HSP70 nucleotide- and peptide-binding family assignments; it differs at five positions from current HSPA6/P17066. The imported Q53FC7 identity is preserved. Its current reference sequence is not an authenticated assay insert, and no autonomous fragment activity, natural-product equivalence or exact full-length insert is asserted. The supplementary insert sequences remain unavailable. Proposed replacements: protein-folding chaperone binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | MODIFY | Summary: The reported Hsp90Ξ² association supports chaperone-partner binding. Reason: The source explicitly measures Hsp90Ξ² interactions by the physical-capture LUMIER assay, and the literal EGFR pair records are positive with their receptor mutations and treatment contexts retained. The paper identifies the partner as a chaperone; the class refinement does not depend on an assumed purified interface. The current Q6PK50 reference is a 351-residue HSP90AB1 fragment. This reference length does not establish that the reported Hsp90Ξ² assay construct was equivalently truncated. The imported Q6PK50 identity is preserved. Its current reference sequence is not an authenticated assay insert, and no autonomous fragment activity, natural-product equivalence or exact full-length insert is asserted. The supplementary insert sequences remain unavailable. Proposed replacements: protein-folding chaperone binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | MODIFY | Summary: The reported Hsc70 association supports chaperone-partner binding. Reason: The source explicitly measures Hsc70 interactions by the physical-capture LUMIER assay, and the literal EGFR pair records are positive with their receptor mutations and treatment contexts retained. The paper identifies the partner as a chaperone; the class refinement does not depend on an assumed purified interface. The current Q96BE0 reference exactly matches HSPA8/P11142 residues 378β646 and retains the HSP70 peptide-binding classification. The imported Q96BE0 identity is preserved. Its current reference sequence is not an authenticated assay insert, and no autonomous fragment activity, natural-product equivalence or exact full-length insert is asserted. The supplementary insert sequences remain unavailable. Proposed replacements: protein-folding chaperone binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The source supports EGFRβERBB2 association with a supported partner-class refinement. Reason: The source abstract and exact curated pair describe endogenous proximity ligation in human HeLa cells. A positive PLA signal establishes close proximity under that assay and alone does not map a direct binding interface. The separately read human EGFR TAP/co-IP source corroborates physical association with ERBB2. The combined evidence supports protein kinase binding while the PLA and corroborating assay contexts remain separate. The original PLA Methods were unavailable after the publisher access failure; no antibody specificity control or full-paper result is invented. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: protein kinase binding |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The source supports EGFRβCDH1 association with a supported partner-class refinement. Reason: The source abstract and exact curated pair describe endogenous proximity ligation in human HeLa cells. A positive PLA signal establishes close proximity under that assay and alone does not map a direct binding interface. The independent MaMTH source contains the exact CDH1 pair. The combined evidence supports cadherin binding while the PLA and corroborating assay contexts remain separate. The original PLA Methods were unavailable after the publisher access failure; no antibody specificity control or full-paper result is invented. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: cadherin binding |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The source supports EGFRβPLCG2 association with a supported partner-class refinement. Reason: The source abstract and exact curated pair describe endogenous proximity ligation in human HeLa cells. A positive PLA signal establishes close proximity under that assay and alone does not map a direct binding interface. The independent MaMTH source contains the exact PLCG2 pair; this is not substituted with the PLCG1 paralog. The combined evidence supports phospholipase binding while the PLA and corroborating assay contexts remain separate. The original PLA Methods were unavailable after the publisher access failure; no antibody specificity control or full-paper result is invented. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: phospholipase binding |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The source supports EGFRβPIK3R1 association with a supported partner-class refinement. Reason: The source abstract and exact curated pair describe endogenous proximity ligation in human HeLa cells. A positive PLA signal establishes close proximity under that assay and alone does not map a direct binding interface. The independent recombinant-domain source measures binding of the PIK3R1 SH2 domain to EGFR phosphopeptides; that domain evidence is not relabeled a native full-length HeLa complex. The combined evidence supports phosphatidylinositol 3-kinase regulatory subunit binding while the PLA and corroborating assay contexts remain separate. The original PLA Methods were unavailable after the publisher access failure; no antibody specificity control or full-paper result is invented. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The source supports EGFRβSTAT3 association with a supported partner-class refinement. Reason: The source abstract and exact curated pair describe endogenous proximity ligation in human HeLa cells. A positive PLA signal establishes close proximity under that assay and alone does not map a direct binding interface. The separately read TAP/co-IP source corroborates the exact STAT3 association. The combined evidence supports DNA-binding transcription factor binding while the PLA and corroborating assay contexts remain separate. The original PLA Methods were unavailable after the publisher access failure; no antibody specificity control or full-paper result is invented. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: The source supports EGFRβPIK3R3 association with a supported partner-class refinement. Reason: The source abstract and exact curated pair describe endogenous proximity ligation in human HeLa cells. A positive PLA signal establishes close proximity under that assay and alone does not map a direct binding interface. The independent MaMTH source contains the exact PIK3R2 pair. The combined evidence supports phosphatidylinositol 3-kinase regulatory subunit binding while the PLA and corroborating assay contexts remain separate. The original PLA Methods were unavailable after the publisher access failure; no antibody specificity control or full-paper result is invented. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding |
| GO:0005515 protein binding | IPI PMID:25594178 A kinase-independent role for EGF receptor in autophagy init... | KEEP AS NON CORE | Summary: Retain the coimmunoprecipitation-supported LAPTM4B association. Reason: Co-IP corroborates the localization observations. The available evidence does not establish a more specific binding-partner class merely from membrane localization or complex facilitation. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25594178 A kinase-independent role for EGF receptor in autophagy init... | KEEP AS NON CORE | Summary: Retain the human RUBCN association. Reason: Human RUBCN records are distinct from the mouse construct records. Its inhibitor role does not make it a catalytic enzyme, and no justified narrower binding term was identified. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25594178 A kinase-independent role for EGF receptor in autophagy init... | KEEP AS NON CORE | Summary: Retain the EXOC4/Sec8 association. Reason: Original co-IP supports the exocyst-subunit association. Complex membership alone does not establish a specific catalytic or signaling-scaffold partner class. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26280537 Secreted and O-GlcNAcylated MIF binds to the human EGF recep... | MODIFY | Summary: EGFR binds the modified cytokine MIF in the reported assay. Reason: Independent official P14174 function establishes the cytokine class. The original supports extracellular O-GlcNAcylated MIF binding; this does not make MIF an EGFR agonist or assign cytokine-receptor signaling to EGFR. Proposed replacements: cytokine binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26551075 EGF-receptor specificity for phosphotyrosine-primed substrat... | MODIFY | Summary: The primed SHC1 substrate peptide reveals phosphotyrosine recognition by EGFR. Reason: PMID26551075 Figure5 and structural Results identify EGFR contacts to the phosphate of SHC1 Tyr240 in a primed substrate peptide. GO:0001784 describes binding to a phosphorylated tyrosine residue within a protein and matches this specific observation. The synthetic peptide maps to P29353 residues345β353 and the p52 sequence coordinates235β243; it is outside the annotated PID and SH2 domains. Preserve the L858R kinase-fragment crystal and separate WT biochemical evidence. This is not SH2/PTB-domain binding, intact scaffold assembly, or proof that all SHC1 natural products act equivalently. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26751287 The LINK-A lncRNA activates normoxic HIF1Ξ± signalling in tri... | MODIFY | Summary: The GPNMB-tagged source supports binding to a signaling scaffold. Reason: The source-specific mechanism links EGFR association with GPNMB to phosphorylation-dependent recruitment of BRK by the GPNMB intracellular region. This measured tethering role supports scaffold protein binding. The imported Q14956-1 identifier is preserved, while reference-sequence identity is not treated as independent authentication of the experimental insert or proof that all GPNMB products behave equivalently. BRK SH2 recognition and LINK-A-mediated organization are separate mechanistic observations. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27059931 Weak binding to E3 ubiquitin ligase c-Cbl increases EGFRvA p... | MODIFY | Summary: The source distinguishes wild-type EGFRβGRB2 binding from loss of detectable binding by EGFRvA. Reason: The verified abstract explicitly contrasts GRB2 association with wild-type receptor and the EGFRvA variant, which failed to bind GRB2 in the reported assay. Independently verified GRB2 tethering of receptor and downstream signaling components supports the scaffold partner class for the positive wild-type assertion. Preserve the imported source without describing EGFRvA as a positive GRB2 binder. The full operative article and insert sequence remain unavailable; no natural-product equivalence or exact SH2 contact is inferred. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | KEEP AS NON CORE | Summary: The source supports EGFRβAMPH association within the measured context. Reason: The original Results identify AMPH among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. The official AMPH account proposes a membrane-associated cytoskeletal role, but the available source set does not resolve a more informative partner class strongly enough for this association. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | KEEP AS NON CORE | Summary: The source supports EGFRβDOK3 association within the measured context. Reason: The original Results identify DOK3 among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. DOK3 is an enzymatically inert signaling adaptor. Its possession of a PTB domain does not establish that domain as the interface in the full-protein co-IP. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | MODIFY | Summary: The source supports EGFRβUSP33 association with a supported partner-class refinement. Reason: The original Results identify USP33 among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. USP33 is a ubiquitin carboxyl-terminal hydrolase with documented deubiquitinating chemistry, supporting the protease partner class. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | KEEP AS NON CORE | Summary: The source supports EGFRβCNKSR2 association within the measured context. Reason: The original Results identify CNKSR2 among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. CNKSR2 is a Ras-pathway scaffold or adaptor, rather than the kinase with which its name associates it. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | MODIFY | Summary: The source supports EGFRβLZTS2 association with a supported partner-class refinement. Reason: The original Results identify LZTS2 among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. LZTS2 regulates katanin-dependent microtubule severing and spindle organization, supporting a cytoskeletal-regulatory partner class. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | KEEP AS NON CORE | Summary: The source supports EGFRβMBIP association within the measured context. Reason: The original Results identify MBIP among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. MBIP is a noncatalytic complex component and kinase inhibitor; those functions do not establish MBIP kinase activity. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27956147 Systematic Identification of Oncogenic EGFR Interaction Part... | MODIFY | Summary: The source supports EGFRβTACC3 association with a supported partner-class refinement. Reason: The original Results identify TACC3 among the eight named proteins confirmed to associate with EGFR-WT by anti-FLAG/GFP coimmunoprecipitation, after a MaMTH screen. Methods describe sequence-verified human ORFeome/MGC-derived clones, HEK293T reporter cells and the tagged-protein co-IP after EGF stimulation. The physical association is distinct from the initial GRB2-translocation phenotype. No exact natural-product insert sequence or native untagged complex is inferred. TACC3 participates structurally in the spindle TACC3βch-TOGβclathrin bridge, supporting a cytoskeletal-protein partner class without transferring microtubule activity to EGFR. Additional TACC3 experiments compare WT and oncogenic EGFR variants and connect association to receptor stabilization; the stronger mutant interaction does not invalidate the WT result. The consulted IntAct export did not contain a matching PMID-specific pair, so the support is the named primary result rather than an invented database join. The refinement states the verified partner class, not transfer of its activity to EGFR. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | MODIFY | Summary: EGFR associates with PTPRA in the reported interaction assay. Reason: The original MaMTH screen identifies EGFRβPTPRA in HEK293T cells. The initial co-IP in Figure 4 did not recover this pair; the Results explicitly report recovery after optimizing the co-IP conditions in Figure S5A. The supplementary procedure itself was not recovered. PTPRA-inactive mutants still reduced EGFR phosphorylation, so that phenotype is not proof of direct PTPRA catalysis on EGFR. The independently captured official PTPRA record establishes the protein-phosphatase partner class; the refinement describes binding to that partner, not its catalytic activity as an EGFR function. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | MODIFY | Summary: EGFR associates with PTPRB in the reported interaction assay. Reason: The original MaMTH screen identifies EGFRβPTPRB in HEK293T cells. Co-IP did not recover the pair under the reported conditions, whereas the membrane two-hybrid signal and cellular phosphorylation experiments were positive. The positive binding assay supports the association without relabeling the functional assay as a purified binary experiment. The independently captured official PTPRB record establishes the protein-phosphatase partner class; the refinement describes binding to that partner, not its catalytic activity as an EGFR function. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | KEEP AS NON CORE | Summary: EGFR associates with SHC1 in the reported interaction assay. Reason: EGFRβSHC1 is the positive control for the original mammalian membrane two-hybrid screen. The separate yeast activity check uses activated EGFR L858R with SHC1, which is not substituted for wild-type receptor in every assay. SHC1 is a noncatalytic adaptor, and this full-protein source does not map a specific SH2/PTB contact. The supported association is retained as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | MODIFY | Summary: EGFR associates with PPM1A in the reported interaction assay. Reason: The inspected Figure 1B contains the positive EGFRβPPM1A MYTH cell, and Figure 4B independently marks this pair as verified by co-IP. The latter uses induced FLAG-phosphatase in Flp-In T-REx HEK293 cells and detects endogenous EGFR. This supports physical association; PPM1A substrate specificity is not inferred from co-purification. The independently captured official PPM1A record establishes the protein-phosphatase partner class; the refinement describes binding to that partner, not its catalytic activity as an EGFR function. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | MODIFY | Summary: EGFR associates with PTPN12 in the reported interaction assay. Reason: The inspected Figure 1B contains the positive EGFRβPTPN12 MYTH cell. The separate quantitative trapping-mutant experiment in Figure 2A explicitly uses EGFR lacking its extracellular region; that engineered activation context is retained rather than described as a native full-length complex. The independently captured official PTPN12 record establishes the protein-phosphatase partner class; the refinement describes binding to that partner, not its catalytic activity as an EGFR function. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | MODIFY | Summary: EGFR associates with PTPN11 in the reported interaction assay. Reason: The inspected Figure 1B contains the positive EGFRβPTPN11 MYTH cell. The source uses replicated membrane two-hybrid screening in yeast with unrelated-bait controls and excludes frequent nonspecific preys. The paper's purified phosphatase experiments on ERBB2/ERBB4 are not transferred to EGFR. The independently captured official PTPN11 record establishes the protein-phosphatase partner class; the refinement describes binding to that partner, not its catalytic activity as an EGFR function. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | MODIFY | Summary: EGFR associates with PTPRH in the reported interaction assay. Reason: The original MaMTH screen identifies EGFRβPTPRH, and the inspected Figure 4B verifies the pair by co-IP of FLAG-tagged PTPRH with endogenous EGFR in human cells. Trapping-mutant and cellular phosphosite experiments further examine the pair, but do not justify transferring phosphatase chemistry to EGFR. The independently captured official PTPRH record establishes the protein-phosphatase partner class; the refinement describes binding to that partner, not its catalytic activity as an EGFR function. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | MODIFY | Summary: EGFR binds the growth factor EGF. Reason: The original reports ligand binding and ligand-induced extracellular receptor dimerization; the exact pair has calorimetry, SAXS and SPR records. The receptor construct is sEGFR501, expressed in Sf9 cells; the paper numbers the extracellular region from the mature chain, whereas the curated sequence interval is 25β525. The assayed human protein is not identified from the insect expression host. EGF binding supplies the exact ligand specificity. No assay of every natural EGFR product is claimed. Proposed replacements: epidermal growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | MODIFY | Summary: EGFR binds the growth factor TGFΞ±. Reason: The original SAXS experiment uses purified extracellular receptor with commercial human TGFΞ± and reports the ligand-bound dimer. The receptor construct is sEGFR501, expressed in Sf9 cells; the paper numbers the extracellular region from the mature chain, whereas the curated sequence interval is 25β525. The assayed human protein is not identified from the insect expression host. Growth factor binding describes this ligand without conflating it with EGF/P01133. No assay of every natural EGFR product is claimed. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | MODIFY | Summary: EGFR binds the growth factor epigen. Reason: The original resolves epigen in the receptor ligand-binding site and measures its binding by calorimetry. The ligand reagent is human Q6UW88 residues E49βY109; a monomeric crystal complex does not mean absent receptor binding. The receptor construct is sEGFR501, expressed in Sf9 cells; the paper numbers the extracellular region from the mature chain, whereas the curated sequence interval is 25β525. The assayed human protein is not identified from the insect expression host. Growth factor binding describes this ligand without conflating it with EGF/P01133. No assay of every natural EGFR product is claimed. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28988771 EGFR Ligands Differentially Stabilize Receptor Dimers to Spe... | MODIFY | Summary: EGFR binds the growth factor HB-EGF. Reason: The original SAXS experiment uses purified extracellular receptor with commercial human HB-EGF. The curated ligand record retains heterogeneous N termini rather than claiming an exactly authenticated full precursor. The receptor construct is sEGFR501, expressed in Sf9 cells; the paper numbers the extracellular region from the mature chain, whereas the curated sequence interval is 25β525. The assayed human protein is not identified from the insect expression host. Growth factor binding describes this ligand without conflating it with EGF/P01133. No assay of every natural EGFR product is claimed. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30083275 The S100A4 Protein Signals through the ErbB4 Receptor to Pro... | MODIFY | Summary: Direct S100A4 association supports S100 protein binding. Reason: The literal partner P26447 is S100A4. Human ectodomain SPR and cross-linking support its binding to EGFR; neither the title nor neuronal ErbB4 dependence negates that positive. Proposed replacements: S100 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | KEEP AS NON CORE | Summary: Retain the measured EGFRβGRB2 association within its source scope. Reason: Curated anti-tag coimmunoprecipitation records cite Figures 5F/G and S7D, retaining the EGFR P1019 mutant effects separately. The independently verified partner is a signaling adaptor. This source does not map a sufficiently specific partner-domain contact to replace the generic binding assertion; an SH2-containing protein is not automatically an isolated SH2 binding reagent. The project-specific policy retains supported generic binding as non-core. The complete publication abstract and detailed curator records were available, but the original full text and supplementary table were not recovered, so additional assay conditions are not asserted. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | KEEP AS NON CORE | Summary: Retain the measured EGFRβSH2B1 association within its source scope. Reason: The literal Q9NRF2 record is human SH2B1, not GAB1. The source-specific anti-bait coimmunoprecipitation record cites Figure 3E after EGF stimulation. The independently verified partner is a signaling adaptor. This source does not map a sufficiently specific partner-domain contact to replace the generic binding assertion; an SH2-containing protein is not automatically an isolated SH2 binding reagent. The project-specific policy retains supported generic binding as non-core. The complete publication abstract and detailed curator records were available, but the original full text and supplementary table were not recovered, so additional assay conditions are not asserted. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | KEEP AS NON CORE | Summary: Retain the measured EGFRβrat Grb7 association within its source scope. Reason: The imported Q9QZC5 is rat Grb7. The source records capture it from rat lysates with biotinylated human EGFR phosphopeptides, including the 1104β1117, 1132β1145 and 1166β1179 intervals; Table S5 also retains local mutation effects. This does not establish a native humanβhuman complex or an isolated SH2-domain assay. The independently verified partner is a signaling adaptor. This source does not map a sufficiently specific partner-domain contact to replace the generic binding assertion; an SH2-containing protein is not automatically an isolated SH2 binding reagent. The project-specific policy retains supported generic binding as non-core. The complete publication abstract and detailed curator records were available, but the original full text and supplementary table were not recovered, so additional assay conditions are not asserted. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31585087 Oncogenic Mutations Rewire Signaling Pathways by Switching P... | KEEP AS NON CORE | Summary: Retain the measured EGFRβGAB2 association within its source scope. Reason: The literal human GAB2 pair has an anti-bait coimmunoprecipitation record at Figure 3C after EGF stimulation. The independently verified partner is a signaling adaptor. This source does not map a sufficiently specific partner-domain contact to replace the generic binding assertion; an SH2-containing protein is not automatically an isolated SH2 binding reagent. The project-specific policy retains supported generic binding as non-core. The complete publication abstract and detailed curator records were available, but the original full text and supplementary table were not recovered, so additional assay conditions are not asserted. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PIK3R2 association to phosphatidylinositol 3-kinase regulatory subunit binding. Reason: The literal PIK3R2βEGFR pair occurs at MYTH Interactome row 275 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PIK3R2 classification supports phosphatidylinositol 3-kinase regulatory subunit binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PIK3C2B association to phosphatidylinositol 3-kinase binding. Reason: The literal PIK3C2BβEGFR pair occurs at MYTH Interactome row 200 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PIK3C2B classification supports phosphatidylinositol 3-kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: phosphatidylinositol 3-kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped LAT association. Reason: The literal LATβEGFR pair occurs at MYTH Interactome row 340 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. LAT is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the TLR2 association to signaling receptor binding. Reason: The literal TLR2βEGFR pair occurs at MYTH Interactome row 339 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official TLR2 classification supports signaling receptor binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the CTNND1 association to cytoskeletal regulatory protein binding. Reason: The literal CTNND1βEGFR pair occurs at MYTH Interactome row 356 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official CTNND1 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped GRAP2 association. Reason: The literal GRAP2βEGFR pair occurs at MYTH Interactome row 257 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. GRAP2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the ABL1 association to protein kinase binding. Reason: The literal ABL1βEGFR pair occurs at MYTH Interactome row 253 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official ABL1 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the TGFA association to growth factor binding. Reason: The literal TGFAβEGFR pair occurs at MYTH Interactome row 406 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official TGFA classification supports growth factor binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the RAF1 association to protein kinase binding. Reason: The literal RAF1βEGFR pair occurs at MYTH Interactome row 283 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official RAF1 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped ANXA1 association. Reason: The literal ANXA1βEGFR pair occurs at MYTH Interactome row 372 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. ANXA1 is a calcium/phospholipid-binding regulatory protein. This record does not justify assigning its calcium-binding property to EGFR or selecting a more specific binding class. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the NR3C1 association to nuclear receptor binding. Reason: The literal NR3C1βEGFR pair occurs at MYTH Interactome row 229 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official NR3C1 classification supports nuclear receptor binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: nuclear receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the GAPDH association to enzyme binding. Reason: The literal GAPDHβEGFR pair occurs at MYTH Interactome row 285 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official GAPDH classification supports enzyme binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the CDK1 association to protein kinase binding. Reason: The literal CDK1βEGFR pair occurs at MYTH Interactome row 369 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official CDK1 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the HSP90AA1 association to Hsp90 protein binding. Reason: The literal HSP90AA1βEGFR pair occurs at MYTH Interactome row 389 (published MYTH/IID integrated network); mtKRAS_Hi interactions row 593 (AP-MS mtKRAS_Hi interactions). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The separately listed AP-MS rows recover the complex in the indicated human colorectal-cell KRAS contexts; co-purification does not map a binary interface. The independently checked official HSP90AA1 classification supports Hsp90 protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the LYN association to protein kinase binding. Reason: The literal LYNβEGFR pair occurs at MYTH Interactome row 217 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official LYN classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the HSP90AB1 association to Hsp90 protein binding. Reason: The literal HSP90AB1βEGFR pair occurs at MYTH Interactome row 350 (published MYTH/IID integrated network); mtKRAS_Hi interactions row 591 (AP-MS mtKRAS_Hi interactions). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The separately listed AP-MS rows recover the complex in the indicated human colorectal-cell KRAS contexts; co-purification does not map a binary interface. The independently checked official HSP90AB1 classification supports Hsp90 protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTPRC association to protein phosphatase binding. Reason: The literal PTPRCβEGFR pair occurs at MYTH Interactome row 207 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. PTPRC is a receptor-type protein tyrosine phosphatase. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the HCK association to protein kinase binding. Reason: The literal HCKβEGFR pair occurs at MYTH Interactome row 222 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official HCK classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the FGR association to protein kinase binding. Reason: The literal FGRβEGFR pair occurs at MYTH Interactome row 358 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official FGR classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the UCHL1 association to protease binding. Reason: The literal UCHL1βEGFR pair occurs at MYTH Interactome row 391 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. UCHL1 is a ubiquitin C-terminal hydrolase/peptidase. Its official record specifically flags disputed ubiquitin-ligase activity, so that alternative class is not used. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protease binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the TXN association to enzyme binding. Reason: The literal TXNβEGFR pair occurs at MYTH Interactome row 302 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official TXN classification supports enzyme binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the HSPA8 association to Hsp70 protein binding. Reason: The literal HSPA8βEGFR pair occurs at MYTH Interactome row 404 (published MYTH/IID integrated network); mtKRAS_Hi interactions row 587 (AP-MS mtKRAS_Hi interactions). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The separately listed AP-MS rows recover the complex in the indicated human colorectal-cell KRAS contexts; co-purification does not map a binary interface. The independently checked official HSPA8 classification supports Hsp70 protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the CDH1 association to cadherin binding. Reason: The literal CDH1βEGFR pair occurs at MYTH Interactome row 329 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official CDH1 classification supports cadherin binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the SRC association to protein kinase binding. Reason: The literal SRCβEGFR pair occurs at MYTH Interactome row 249 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official SRC classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped JUP association. Reason: The literal JUPβEGFR pair occurs at MYTH Interactome row 203 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. JUP is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the EZR association to cytoskeletal protein binding. Reason: The literal EZRβEGFR pair occurs at MYTH Interactome row 274 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official EZR classification supports cytoskeletal protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped MUC1 association. Reason: The literal MUC1βEGFR pair occurs at MYTH Interactome row 280 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. MUC1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PDGFRA association to protein kinase binding. Reason: The literal PDGFRAβEGFR pair occurs at MYTH Interactome row 336 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PDGFRA classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped NCK1 association. Reason: The literal NCK1βEGFR pair occurs at MYTH Interactome row 224 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. NCK1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PLCG2 association to phospholipase binding. Reason: The literal PLCG2βEGFR pair occurs at MYTH Interactome row 265 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PLCG2 classification supports phospholipase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: phospholipase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the GOT1 association to enzyme binding. Reason: The literal GOT1βEGFR pair occurs at MYTH Interactome row 327 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. GOT1 is a cytosolic aspartate aminotransferase with documented catalytic activity. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PRKCA association to protein kinase binding. Reason: The literal PRKCAβEGFR pair occurs at MYTH Interactome row 365 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PRKCA classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTPN1 association to protein phosphatase binding. Reason: The literal PTPN1βEGFR pair occurs at MYTH Interactome row 378 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PTPN1 classification supports protein phosphatase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTPRA association to protein phosphatase binding. Reason: The literal PTPRAβEGFR pair occurs at MYTH Interactome row 258 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. PTPRA is a receptor-type protein tyrosine phosphatase. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTPRB association to protein phosphatase binding. Reason: The literal PTPRBβEGFR pair occurs at MYTH Interactome row 386 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. PTPRB is a receptor-type protein tyrosine phosphatase. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTPRG association to protein phosphatase binding. Reason: The literal PTPRGβEGFR pair occurs at MYTH Interactome row 397 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. PTPRG is a receptor-type protein tyrosine phosphatase. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the CFL1 association to cytoskeletal regulatory protein binding. Reason: The literal CFL1βEGFR pair occurs at MYTH Interactome row 225 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official CFL1 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped S100A4 association. Reason: The literal S100A4βEGFR pair occurs at MYTH Interactome row 345 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. S100A4 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the YWHAQ association to 14-3-3 protein binding. Reason: The literal YWHAQβEGFR pair occurs at MYTH Interactome row 360 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official YWHAQ classification supports 14-3-3 protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped SHC1 association. Reason: The literal SHC1βEGFR pair occurs at MYTH Interactome row 219 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. SHC1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the AKT1 association to protein kinase binding. Reason: The literal AKT1βEGFR pair occurs at MYTH Interactome row 276 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official AKT1 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the SFN association to 14-3-3 protein binding. Reason: The literal SFNβEGFR pair occurs at MYTH Interactome row 231 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official SFN classification supports 14-3-3 protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped STIP1 association. Reason: The literal STIP1βEGFR pair occurs at MYTH Interactome row 385 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. STIP1 mediates HSP70βHSP90 association as a co-chaperone. The captured official record does not itself establish the nascent/unfolded client-binding property used to select GO:0051087, so no chaperone-class refinement is forced. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the ARRB2 association to arrestin family protein binding. Reason: The literal ARRB2βEGFR pair occurs at MYTH Interactome row 277 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official ARRB2 classification supports arrestin family protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: arrestin family protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped HSPA4 association. Reason: The literal HSPA4βEGFR pair occurs at MYTH Interactome row 307 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. HSPA4 is identified as a heat-shock protein in the official record, but the saved record lacks a FUNCTION account establishing the specific nascent/unfolded-client-handling property needed for a chaperone-class refinement. The positive pair is retained as non-core under the project policy. This uncertainty concerns the partner classification, not a requirement to demonstrate that EGFR is a folding client or to map a purified interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the HSPA9 association to Hsp70 protein binding. Reason: The literal HSPA9βEGFR pair occurs at MYTH Interactome row 296 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. HSPA9 is an Hsp70-family chaperone with documented protein import, folding and refolding functions; mitochondrial enrichment does not negate an experimentally recorded association in another assay context. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: Hsp70 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the STAT3 association to DNA-binding transcription factor binding. Reason: The literal STAT3βEGFR pair occurs at MYTH Interactome row 402 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official STAT3 classification supports DNA-binding transcription factor binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the STAT1 association to DNA-binding transcription factor binding. Reason: The literal STAT1βEGFR pair occurs at MYTH Interactome row 355 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official STAT1 classification supports DNA-binding transcription factor binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the STAT5A association to DNA-binding transcription factor binding. Reason: The literal STAT5AβEGFR pair occurs at MYTH Interactome row 272 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official STAT5A classification supports DNA-binding transcription factor binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the ABL2 association to protein kinase binding. Reason: The literal ABL2βEGFR pair occurs at MYTH Interactome row 344 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official ABL2 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the ZAP70 association to protein kinase binding. Reason: The literal ZAP70βEGFR pair occurs at MYTH Interactome row 284 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official ZAP70 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped CRK association. Reason: The literal CRKβEGFR pair occurs at MYTH Interactome row 212 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. CRK is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped CRKL association. Reason: The literal CRKLβEGFR pair occurs at MYTH Interactome row 294 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. CRKL is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped CAMLG association. Reason: The literal CAMLGβEGFR pair occurs at MYTH Interactome row 349 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. CAMLG is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the ARRB1 association to arrestin family protein binding. Reason: The literal ARRB1βEGFR pair occurs at MYTH Interactome row 343 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official ARRB1 classification supports arrestin family protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: arrestin family protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the BLK association to protein kinase binding. Reason: The literal BLKβEGFR pair occurs at MYTH Interactome row 392 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official BLK classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped CAV2 association. Reason: The literal CAV2βEGFR pair occurs at MYTH Interactome row 381 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. CAV2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped GABARAPL2 association. Reason: The literal GABARAPL2βEGFR pair occurs at MYTH Interactome row 316 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. GABARAPL2 is an autophagy-related ubiquitin-like modifier, not the conjugating enzyme that acts on it. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped GRB2 association. Reason: The literal GRB2βEGFR pair occurs at MYTH Interactome row 382 (published MYTH/IID integrated network); mtKRAS_Hi interactions row 918 (AP-MS mtKRAS_Hi interactions); mtKRAS_Lo interactions row 748 (AP-MS mtKRAS_Lo interactions). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The separately listed AP-MS rows recover the complex in the indicated human colorectal-cell KRAS contexts; co-purification does not map a binary interface. GRB2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the YWHAZ association to 14-3-3 protein binding. Reason: The literal YWHAZβEGFR pair occurs at MYTH Interactome row 204 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official YWHAZ classification supports 14-3-3 protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: 14-3-3 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped AKAP12 association. Reason: The literal AKAP12βEGFR pair occurs at MYTH Interactome row 279 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. AKAP12 is a kinase-anchoring scaffold, not the protein kinase it recruits. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped CAV1 association. Reason: The literal CAV1βEGFR pair occurs at MYTH Interactome row 371 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. CAV1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTPN12 association to protein phosphatase binding. Reason: The literal PTPN12βEGFR pair occurs at MYTH Interactome row 380 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PTPN12 classification supports protein phosphatase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTK2 association to protein kinase binding. Reason: The literal PTK2βEGFR pair occurs at MYTH Interactome row 211 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PTK2 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped AHNAK association. Reason: The literal AHNAKβEGFR pair occurs at MYTH Interactome row 328 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. AHNAK is a large scaffold with multiple reported cellular roles; the saved class evidence does not resolve a narrower binding class for this association. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the MAP3K12 association to protein kinase binding. Reason: The literal MAP3K12βEGFR pair occurs at MYTH Interactome row 234 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. MAP3K12 is a catalytically active protein kinase. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the EPS8 association to cytoskeletal regulatory protein binding. Reason: The literal EPS8βEGFR pair occurs at MYTH Interactome row 215 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official EPS8 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the TRAF2 association to ubiquitin protein ligase binding. Reason: The literal TRAF2βEGFR pair occurs at MYTH Interactome row 311 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The TRAF2 ubiquitin-ligase classification is supported by its explicit official catalytic annotation and a recombinant-protein experiment, not merely its name or recruitment of cIAP ligases. PMID:20577214 reports S1P-dependent TRAF2-mediated RIP1 ubiquitination with E1/E2, RING-deletion and linkage controls, and separately excludes cIAP1/2 and TRAF5 from the tested preparation. Thus GO:0031625 describes binding to a partner with demonstrated conditional E3 activity. It does not assign ubiquitination to EGFR or claim that TRAF2 acts catalytically in this interaction assay; TRAF2 also has distinct cIAP-recruitment roles. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped LCP2 association. Reason: The literal LCP2βEGFR pair occurs at MYTH Interactome row 379 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. LCP2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped SLA association. Reason: The literal SLAβEGFR pair occurs at MYTH Interactome row 317 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. SLA is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped GRB10 association. Reason: The literal GRB10βEGFR pair occurs at MYTH Interactome row 338 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. GRB10 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped MAPK8IP2 association. Reason: The literal MAPK8IP2βEGFR pair occurs at MYTH Interactome row 208 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. MAPK8IP2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped GAB1 association. Reason: The literal GAB1βEGFR pair occurs at MYTH Interactome row 373 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. GAB1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the CTTN association to cytoskeletal regulatory protein binding. Reason: The literal CTTNβEGFR pair occurs at MYTH Interactome row 374 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official CTTN classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the FKBP8 association to enzyme binding. Reason: The literal FKBP8βEGFR pair occurs at MYTH Interactome row 341 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. FKBP8 has directly supported peptidyl-prolyl isomerase activity that is conditional on calcium/calmodulin. This is enzyme-class binding, not a claim of constitutive activity in the interaction assay. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped TAB1 association. Reason: The literal TAB1βEGFR pair occurs at MYTH Interactome row 401 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. TAB1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the CDC37 association to protein-folding chaperone binding. Reason: The literal CDC37βEGFR pair occurs at mtKRAS_Hi interactions row 584 (AP-MS mtKRAS_Hi interactions); mtKRAS_Lo interactions row 497 (AP-MS mtKRAS_Lo interactions). The separately listed AP-MS rows recover the complex in the indicated human colorectal-cell KRAS contexts; co-purification does not map a binary interface. CDC37 contacts kinase clients and stabilizes an unfolded kinase intermediate in the human HSP90βCDC37βCDK4 structure (PMID:27339980). This supports the chaperone partner class without requiring EGFR itself to perform folding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein-folding chaperone binding |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the NTRK2 association to protein kinase binding. Reason: The literal NTRK2βEGFR pair occurs at MYTH Interactome row 244 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official NTRK2 classification supports protein kinase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the TNS3 association to cytoskeletal regulatory protein binding. Reason: The literal TNS3βEGFR pair occurs at MYTH Interactome row 362 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official TNS3 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped SHC4 association. Reason: The literal SHC4βEGFR pair occurs at MYTH Interactome row 384 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. SHC4 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the TUBA1A association to tubulin binding. Reason: The literal TUBA1AβEGFR pair occurs at MYTH Interactome row 300 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official TUBA1A classification supports tubulin binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: tubulin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the HDAC7 association to histone deacetylase binding. Reason: The literal HDAC7βEGFR pair occurs at MYTH Interactome row 323 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official HDAC7 classification supports histone deacetylase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: histone deacetylase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PIK3R3 association to phosphatidylinositol 3-kinase regulatory subunit binding. Reason: The literal PIK3R3βEGFR pair occurs at MYTH Interactome row 271 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PIK3R3 classification supports phosphatidylinositol 3-kinase regulatory subunit binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped ANKS1A association. Reason: The literal ANKS1AβEGFR pair occurs at MYTH Interactome row 227 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. ANKS1A is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped APBB2 association. Reason: The literal APBB2βEGFR pair occurs at MYTH Interactome row 269 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. APBB2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped AP2M1 association. Reason: The literal AP2M1βEGFR pair occurs at MYTH Interactome row 223 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. AP2M1 is a cargo-adaptor complex subunit; a specific cargo-recognition interface is not mapped by this network record. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped SH2D3A association. Reason: The literal SH2D3AβEGFR pair occurs at MYTH Interactome row 383 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. SH2D3A is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped SH2B1 association. Reason: The literal SH2B1βEGFR pair occurs at MYTH Interactome row 400 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. SH2B1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped CISH association. Reason: The literal CISHβEGFR pair occurs at MYTH Interactome row 398 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. CISH is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped ITSN2 association. Reason: The literal ITSN2βEGFR pair occurs at MYTH Interactome row 243 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. ITSN2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the source-scoped VAPA association. Reason: The literal VAPAβEGFR pair occurs at MYTH Interactome row 291 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. VAPA is a membrane-contact-site/vesicle-associated protein; it is not classified as a SNARE solely from its name. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the HDAC6 association to enzyme binding. Reason: The literal HDAC6βEGFR pair occurs at MYTH Interactome row 267 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official HDAC6 classification supports enzyme binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the STUB1 association to ubiquitin protein ligase binding. Reason: The literal STUB1βEGFR pair occurs at MYTH Interactome row 326 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official STUB1 classification supports ubiquitin protein ligase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the WASF3 association to cytoskeletal regulatory protein binding. Reason: The literal WASF3βEGFR pair occurs at MYTH Interactome row 292 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official WASF3 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the BAIAP2 association to cytoskeletal regulatory protein binding. Reason: The literal BAIAP2βEGFR pair occurs at MYTH Interactome row 342 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official BAIAP2 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the MAST1 association to protein kinase binding. Reason: The literal MAST1βEGFR pair occurs at MYTH Interactome row 351 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. MAST1 is a serine/threonine protein kinase. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: Refine the PTPN22 association to protein phosphatase binding. Reason: The literal PTPN22βEGFR pair occurs at MYTH Interactome row 256 (published MYTH/IID integrated network). Supplementary Methods30 explicitly integrates earlier EGFR MYTH and IID evidence; the new MYTH screens in this paper target ERBB2/3/4. The network row is therefore not mislabeled as a newly measured EGFR binary assay or an AP-MS result. The independently checked official PTPN22 classification supports protein phosphatase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | KEEP AS NON CORE | Summary: EGFR co-purifies with SOS1 in the published cancer-network dataset. Reason: The publication-linked NDEx deposit contains the exact EGFRβSOS1 edge and accession pair, with positive detection labels for HET1A. The main original describes triplicate inducible FLAG-bait affinity purification and mass spectrometry in two head-and-neck cancer lines and an immortalized comparator. These are physical co-complex measurements, not BioID-only proximity or a purified binary interface. The network also contains database-only edges, which are kept distinct; this selected edge has experimental detection labels. SOS1 is a Ras guanine-nucleotide exchange factor. Its exchange activity is not transferred to EGFR, and the association alone does not establish a more specific EGFR adaptor or exchange-regulator activity. Retain the supported association as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | KEEP AS NON CORE | Summary: EGFR co-purifies with OS9 in the published cancer-network dataset. Reason: The publication-linked NDEx deposit contains the exact EGFRβOS9 edge and accession pair, with positive detection labels for SCC25, HET1A, CAL33. The main original describes triplicate inducible FLAG-bait affinity purification and mass spectrometry in two head-and-neck cancer lines and an immortalized comparator. These are physical co-complex measurements, not BioID-only proximity or a purified binary interface. The network also contains database-only edges, which are kept distinct; this selected edge has experimental detection labels. OS9 recognizes improperly folded glycoproteins and delivers them toward ER-associated degradation. Recognition for degradation alone does not establish the folding or transport chaperone property required for GO:0051087. Retain the supported association as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | MODIFY | Summary: EGFR co-purifies with TNS4 in the published cancer-network dataset. Reason: The publication-linked NDEx deposit contains the exact EGFRβTNS4 edge and accession pair, with positive detection labels for SCC25. The main original describes triplicate inducible FLAG-bait affinity purification and mass spectrometry in two head-and-neck cancer lines and an immortalized comparator. These are physical co-complex measurements, not BioID-only proximity or a purified binary interface. The network also contains database-only edges, which are kept distinct; this selected edge has experimental detection labels. The independently captured official TNS4 record describes displacement of TNS3 from integrins and consequent actin stress-fiber disassembly. This supports the cytoskeletal-regulatory partner class without assigning actin binding or phosphatase chemistry to EGFR. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591642 A protein network map of head and neck cancer reveals PIK3CA... | KEEP AS NON CORE | Summary: EGFR co-purifies with ERRFI1 in the published cancer-network dataset. Reason: The publication-linked NDEx deposit contains the exact EGFRβERRFI1 edge and accession pair, with positive detection labels for HET1A. The main original describes triplicate inducible FLAG-bait affinity purification and mass spectrometry in two head-and-neck cancer lines and an immortalized comparator. These are physical co-complex measurements, not BioID-only proximity or a purified binary interface. The network also contains database-only edges, which are kept distinct; this selected edge has experimental detection labels. ERRFI1 is a noncatalytic receptor regulator. Its inhibitory role does not make it a protein kinase or phosphatase, and the AP-MS record does not itself map a binding-specific regulatory mechanism. Retain the supported association as non-core under the project-specific generic-binding policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal ANXA2βEGFR pair at EV1A row 7758 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. The independently indexed complete abstract of PMID:25136068 explicitly reports a complex containing EGFR, ANXA2 and the microbial p37 protein in the gastric-cancer infection study. This supports a physical co-complex association in that context, although its full operative assay details have not been recovered. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal JUPβEGFR pair at EV1A row 7712 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. The independently verified human-cell MaMTH dataset in PMID:24658140 contains the EGFRβJUP pair. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the EZR association to cytoskeletal protein binding. Reason: Dataset EV1A contains the literal EZRβEGFR pair at EV1A row 7741 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This row is BioID-only and establishes proximity under the labeling conditions, not a purified binary contact. Independently read PMID:24658140 reports the same partner in a positive MaMTH association (source row 711); the narrower class uses that corroboration as well as this proximity record. The independently checked official EZR classification supports cytoskeletal protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal protein binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal NCK1βEGFR pair at EV1A row 7804 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. The independently verified MaMTH dataset in PMID:24658140 contains the EGFRβNCK1 pair; the isolated NCK1 SH2 experiment in PMID:16273093 is a separate, narrower fragment result. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the PTPN1 association to protein phosphatase binding. Reason: Dataset EV1A contains the literal PTPN1βEGFR pair at EV1A row 7811 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This row is BioID-only and establishes proximity under the labeling conditions, not a purified binary contact. Independently read PMID:24658140 reports the same partner in a positive MaMTH association (source row 717); the narrower class uses that corroboration as well as this proximity record. The independently checked official PTPN1 classification supports protein phosphatase binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the PIK3R1 association to phosphatidylinositol 3-kinase regulatory subunit binding. Reason: Dataset EV1A contains the literal PIK3R1βEGFR pair at EV1A row 7857 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This row is BioID-only and establishes proximity under the labeling conditions, not a purified binary contact. Independently read PMID:16273093 directly measures binding of this partnerβs isolated SH2 domain to EGFR phosphopeptides; that domain assay corroborates the interaction, without authenticating a full-length insert in BioID. PIK3R1 is a PI3K regulatory subunit, not its catalytic p110 partner. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: phosphatidylinositol 3-kinase regulatory subunit binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped SHC1 association. Reason: Dataset EV1A contains the literal SHC1βEGFR pair at EV1A row 2751 (AP); EV1A row 7774 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. SHC1 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the GABRA2 association to transmembrane transporter binding. Reason: Dataset EV1A contains the literal GABRA2βEGFR pair at EV1A row 2776 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. GABRA2 is a pore-forming alpha subunit of the GABA-gated chloride-channel complex. The transporter-binding definition includes transporter proteins and protein complexes; it does not imply EGFR conducts chloride. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal NUMBβEGFR pair at EV1A row 7734 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. PMID:16273093 independently measures binding between EGFR phosphopeptides and the isolated NUMB PTB domain. That establishes a biochemical binding capability, while neither experiment demonstrates the native full-length complex or makes all products equivalent. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the SEC61A1 association to transmembrane transporter binding. Reason: Dataset EV1A contains the literal SEC61A1βEGFR pair at EV1A row 2772 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. SEC61A1 forms the gated pore of the SEC61 translocon that transports precursor polypeptides across the ER membrane. The class concerns this transporter subunit, not transport activity of EGFR. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped GRB2 association. Reason: Dataset EV1A contains the literal GRB2βEGFR pair at EV1A row 2749 (AP); EV1A row 7784 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. GRB2 is a signaling/adaptor or regulatory partner for which this source does not establish a more informative binding class or a domain-specific interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the PTPN11 association to protein phosphatase binding. Reason: Dataset EV1A contains the literal PTPN11βEGFR pair at EV1A row 1545 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This row is BioID-only and establishes proximity under the labeling conditions, not a purified binary contact. Independently read PMID:16273093 directly measures binding of this partnerβs isolated SH2 domain to EGFR phosphopeptides; that domain assay corroborates the interaction, without authenticating a full-length insert in BioID. PTPN11 is a protein tyrosine phosphatase; the binding assay does not transfer phosphatase activity to EGFR. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein phosphatase binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped AP1B1 association. Reason: Dataset EV1A contains the literal AP1B1βEGFR pair at EV1A row 2740 (AP); EV1A row 7782 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. AP1B1 is a subunit of a vesicular cargo-adaptor complex, not itself a catalytic enzyme. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the EPS8 association to cytoskeletal regulatory protein binding. Reason: Dataset EV1A contains the literal EPS8βEGFR pair at EV1A row 7872 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This row is BioID-only and establishes proximity under the labeling conditions, not a purified binary contact. Independently read PMID:24658140 reports the same partner in a positive MaMTH association (source row 743); the narrower class uses that corroboration as well as this proximity record. The independently checked official EPS8 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped OS9 association. Reason: Dataset EV1A contains the literal OS9βEGFR pair at EV1A row 2767 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. OS9 is an ER quality-control lectin that recognizes misfolded glycoproteins and delivers them toward ERAD. Recognition for degradation alone does not establish the folding/transport chaperone property in GO:0051087. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal GAB1βEGFR pair at EV1A row 7763 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. The independently verified human-cell MaMTH dataset in PMID:24658140 contains the EGFRβGAB1 pair. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the TUBB2A association to tubulin binding. Reason: Dataset EV1A contains the literal TUBB2AβEGFR pair at EV1A row 2735 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. TUBB2A is a beta-tubulin constituent of microtubules. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: tubulin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the ERBB4 association to protein kinase binding. Reason: Dataset EV1A contains the literal ERBB4βEGFR pair at EV1A row 2744 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. ERBB4 is a receptor protein tyrosine kinase. The accession-level association is not proof of identical interactions or catalytic behavior for every ERBB4 alternative product. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal TAB1βEGFR pair at EV1A row 7853 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. The independently verified human-cell MaMTH dataset in PMID:24658140 contains the EGFRβTAB1 pair. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the CDC37 association to protein-folding chaperone binding. Reason: Dataset EV1A contains the literal CDC37βEGFR pair at EV1A row 2746 (AP); EV1A row 7786 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. CDC37 contacts kinase clients and stabilizes an unfolded kinase intermediate in the human HSP90βCDC37βCDK4 structure (PMID:27339980). This supports the chaperone partner class without requiring EGFR itself to perform folding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: protein-folding chaperone binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal ANKS1AβEGFR pair at EV1A row 7718 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. The independently verified human-cell MaMTH dataset in PMID:24658140 contains the EGFRβANKS1A pair; the isolated PTB-domain result in PMID:16273093 is a separate, narrower experiment. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped AP2M1 association. Reason: Dataset EV1A contains the literal AP2M1βEGFR pair at EV1A row 2742 (AP); EV1A row 7772 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. AP2M1 is a cargo-adaptor complex subunit; a specific cargo-recognition interface is not mapped by this network record. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped FANCD2 association. Reason: Dataset EV1A contains the literal FANCD2βEGFR pair at EV1A row 2766 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. FANCD2 is a DNA-repair-associated protein; binding to it does not establish EGFR DNA binding, nuclease activity or a more specific binding interface. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal ITSN2βEGFR pair at EV1A row 7771 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. The independently verified human-cell MaMTH dataset in PMID:24658140 contains the EGFRβITSN2 pair. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal VAPAβEGFR pair at EV1A row 7822 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. PMID:20029029 independently reports the EGFRβVAPA MYTH pair, with a source-linked coimmunoprecipitation record at supplementary FigureS3C. The main MYTH construct is human EGFR25β1210 expressed with a yeast secretion signal, so this does not prove a native human interface. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped SEL1L association. Reason: Dataset EV1A contains the literal SEL1LβEGFR pair at EV1A row 2753 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. SEL1L is a noncatalytic ERAD-complex component, not the ubiquitin ligase associated with that complex. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Retain the source-scoped ERRFI1 association. Reason: Dataset EV1A contains the literal ERRFI1βEGFR pair at EV1A row 2748 (AP). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. The AP result supports co-complex association; accompanying BioID, where present, supplies a distinct proximity measurement. Neither method by itself specifies a direct interface. ERRFI1 is a receptor-feedback inhibitor, not a kinase or phosphatase by virtue of inhibiting receptor phosphorylation. Retain the supported curated association under the project-specific generic-binding policy; this is not a claim of contamination or biological noninteraction. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal APPL1βEGFR pair at EV1A row 7838 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. PMID:16273093 independently measures EGFR-phosphopeptide binding by the isolated APPL1 PTB domain. This is biochemical binding evidence at fragment level, not authentication of a native full-length complex. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | MODIFY | Summary: Refine the BAIAP2 association to cytoskeletal regulatory protein binding. Reason: Dataset EV1A contains the literal BAIAP2βEGFR pair at EV1A row 7768 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This row is BioID-only and establishes proximity under the labeling conditions, not a purified binary contact. Independently read PMID:24658140 reports the same partner in a positive MaMTH association (source row 767); the narrower class uses that corroboration as well as this proximity record. The independently checked official BAIAP2 classification supports cytoskeletal regulatory protein binding. The refinement describes the verified partner class, not transferred partner chemistry or an unmeasured endogenous physiological interaction. Proposed replacements: cytoskeletal regulatory protein binding |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | KEEP AS NON CORE | Summary: Binding is independently supported; the cited atlas measures proximity. Reason: Dataset EV1A contains the literal NUMBLβEGFR pair at EV1A row 7773 (BIOID). Human MAC-tagged EGFR in Flp-In293 T-REx cells was assessed by separate affinity-purification and proximity-labeling workflows; the exact source-method labels are retained. This source-specific BioID result establishes proximity, which alone is insufficient to demonstrate protein binding. PMID:16273093 independently measures EGFR-phosphopeptide binding by the isolated NUMBL PTB domain. This is biochemical binding evidence at fragment level, not authentication of a native full-length complex. Retain the generic binding assertion as non-core on the combined positive evidence, while preserving the distinction between the BioID observation and its independent corroboration. The project-specific retention policy determines the disposition of supported generic binding; it is not itself evidence that an interaction occurred. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβESR1 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official ESR1 record supports the nuclear receptor binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: nuclear receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβRAF1 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official RAF1 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβHSP90AA1 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official HSP90AA1 record supports the Hsp90 protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: Hsp90 protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβSRC association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official SRC record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβPLCG2 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. This pair is specifically recorded as an interaction caused by EGFR L858R; it supports the tested mutant context and does not establish the same interaction for wild-type EGFR. The literal partner is PLCG2, a phospholipase, rather than the PLCG1 paralog. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: phospholipase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβGOT1 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official GOT1 record supports the enzyme binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβERBB3 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. ERBB3 is a signaling receptor with limited kinase activity; the receptor-binding class avoids attributing its heterodimer partner's stronger catalytic activity to it. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: signaling receptor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβAXL association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. This pair is specifically recorded as an interaction caused by EGFR L858R; it supports the tested mutant context and does not establish the same interaction for wild-type EGFR. The independently checked official AXL record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβAKT1 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The records separately include AKT1 E17K and EGFR L858R comparisons. The independently checked official AKT1 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβARRB2 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official ARRB2 record supports the arrestin family protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: arrestin family protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβSTAT3 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official STAT3 record supports the DNA-binding transcription factor binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβSYK association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official SYK record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβARRB1 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official ARRB1 record supports the arrestin family protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: arrestin family protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβPTPN11 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The records separately include PTPN11 A72V and EGFR L858R comparisons. The independently checked official PTPN11 record supports the protein phosphatase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβPTK6 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. This pair is specifically recorded as an interaction caused by EGFR L858R; it supports the tested mutant context and does not establish the same interaction for wild-type EGFR. The independently checked official PTK6 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | KEEP AS NON CORE | Summary: The source supports EGFRβBECN1 association within its assay context. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. BECN1 is a noncatalytic organizing component of class III phosphatidylinositol 3-kinase complexes; complex membership does not make it the kinase. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβERBB4 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. This pair is specifically recorded as an interaction caused by EGFR L858R; it supports the tested mutant context and does not establish the same interaction for wild-type EGFR. The independently checked official ERBB4 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβNTRK2 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. This pair is specifically recorded as an interaction caused by EGFR L858R; it supports the tested mutant context and does not establish the same interaction for wild-type EGFR. The independently checked official NTRK2 record supports the protein kinase binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | KEEP AS NON CORE | Summary: The source supports EGFRβRUBCN association within its assay context. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. This pair is specifically recorded as an interaction caused by EGFR L858R; it supports the tested mutant context and does not establish the same interaction for wild-type EGFR. RUBCN regulates class III phosphatidylinositol 3-kinase and phagocytic complexes; these roles do not establish an enzyme class for RUBCN itself. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | KEEP AS NON CORE | Summary: The source supports EGFRβFANCD2 association within its assay context. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. FANCD2 is a DNA-repair complex component; this association does not establish a narrower DNA-binding transcription-factor or enzyme partner class. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | KEEP AS NON CORE | Summary: The source supports EGFRβMBIP association within its assay context. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. MBIP is a component of the ATAC complex and can inhibit protein kinases. Neither property makes MBIP the catalytic kinase. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | KEEP AS NON CORE | Summary: The source supports EGFRβERRFI1 association within its assay context. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. ERRFI1 is a receptor-associated inhibitor; inhibition of a kinase is distinct from possessing kinase activity. The supported generic association is retained as non-core under the project-specific policy. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: The source supports EGFRβWASF3 association with a partner-class refinement. Reason: The source measures tagged protein associations by quantitative BRET in human HEK293T cells, with saturation titrations and donor/acceptor controls. The literal positive pair is retained with its curated construct features and supplementary-table locator. The selected records include engineered mutation comparisons; a recorded mutation having no effect is not evidence of nonbinding. These data do not establish an endogenous complex or equivalence of natural truncated products. The independently checked official WASF3 record supports the cytoskeletal regulatory protein binding partner class. The refinement describes the binding partner class and does not transfer partner catalysis or a downstream pathway role to EGFR. Proposed replacements: cytoskeletal regulatory protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7518560 Hierarchy of binding sites for Grb2 and Shc on the epidermal... | MODIFY | Summary: Direct Grb2 SH2 docking is distinguished from indirect Shc-mediated association. Reason: The source supports direct Grb2 recognition at EGFR Y1068/Y1086 and separately describes indirect association through Shc at Y1173. SH2 domain binding describes the direct component; do not present every recovered Grb2βreceptor association as a direct contact at every site. Proposed replacements: SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7657591 Tyrosine phosphorylation of the c-cbl proto-oncogene protein... | MODIFY | Summary: The mouse Cbl/human EGFR association supports an E3-ligase partner class. Reason: Two literal IntAct co-immunoprecipitation records identify mouse P22682 paired with human EGFR in NIH3T3 cells. Current mouse Cbl is independently classified as an E3 ubiquitin ligase. Retain that species and physical-association scope, without substituting human CBL or asserting direct binary contact/catalysis. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7693694 Sequence specificity in recognition of the epidermal growth ... | MODIFY | Summary: The source resolves substrate recognition by rat PTP1. Reason: The original rat PTP1-C215S and EGFR-mutant/phosphopeptide experiments support protein phosphatase binding. Preserve P20417 and the engineered substrate-trapping context; neither the host nor the homologous human phosphatase changes the literal participant. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9020117 Subsets of epidermal growth factor receptors during activati... | MODIFY | Summary: Grb2-associated receptor pools support binding to a scaffold-class partner. Reason: The original reports positive Grb2 association across compared receptor pools; reduced relative recovery is not a negative interaction. Independently documented GRB2 tethering of pathway members supports scaffold protein binding. This row does not isolate a Grb2 domain or assign scaffold activity to EGFR. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9135143 Activation of HER4 by heparin-binding EGF-like growth factor... | MODIFY | Summary: The HER1 control supports binding to the distinct growth factor HB-EGF. Reason: The complete abstract explicitly reports HB-EGF binding to HER1/EGFR. Q99075 identifies HB-EGF, a growth factor distinct from the EGF protein, so growth factor binding is the supported class refinement. Exact ligand species/production and full Methods remain unresolved; HER4-specific outcomes are not transferred. Proposed replacements: growth factor binding Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR occupies the cell surface in the EGF-binding and internalization experiment. Reason: The original radioligand binding and acid-wash internalization experiments distinguish surface-bound from internalized EGF in HeLa cells. Membrane-impermeable crosslinking and surface-receptor measurements support plasma-membrane localization. The source does not claim that the receptor remains exclusively at the surface. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:15611079 Epigen, the last ligand of ErbB receptors, reveals intricate... | ACCEPT | Summary: The epigen study examines cell-surface EGFR ligand responses. Reason: The abstract reports ligand binding, receptor-mediated ligand depletion and receptor down-regulation in cells expressing ERBB1/EGFR. These are consistent with the established plasma-membrane receptor pool. The original full Methods were unavailable, so no specific assay-cell species or expression-construct sequence is asserted. |
| GO:0005886 plasma membrane | IDA PMID:20462955 A G{alpha}i-GIV molecular complex binds epidermal growth fac... | ACCEPT | Summary: EGF-bound EGFR is directly tracked at the plasma membrane. Reason: The study follows endogenous EGFR in human HeLa cells using HRP-EGF, surface/permeabilized staining and endosomal imaging. GIV perturbations alter receptor retention and internalization. This provides source-specific evidence for the plasma-membrane receptor pool, rather than inferring location solely from a transmembrane segment; it does not make every later intracellular pool equivalent. Supporting Evidence: |
| GO:0007173 epidermal growth factor receptor signaling pathway | IDA PMID:9890893 Identification of tyrosine phosphorylation sites in human Ga... | ACCEPT | Summary: EGFR phosphorylates a docking protein within its signaling pathway. Reason: The complete source abstract reports direct phosphorylation of recombinant human GAB1 by WGA-purified EGFR and a recombinant receptor kinase domain, followed by phosphosite mapping and phosphotyrosine-dependent recruitment of Syp. This establishes an active signaling step. Unavailable full Methods do not justify additional construct-species or native stoichiometry claims. Supporting Evidence: |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:23418353 The E3 ubiquitin ligases RNF126 and Rabring7 regulate endoso... | ACCEPT | Summary: EGFR associates with the E3 ubiquitin ligase RNF115/Rabring7. Reason: The verified PMID:23418353 abstract explicitly reports Rabring7 association with EGFR and promotion of receptor ubiquitination, with a distinct depletion/sorting experiment in HeLa cells. The imported Q9D0C1 identifier denotes mouse Rnf115 and remains unchanged; its official record supports the ligase partner class. Full original Methods were not recovered, so species and insert details are not inferred from the human host cell. Retain this binding assertion without attributing the partnerβs ubiquitin-transfer reaction to EGFR. Supporting Evidence: |
| GO:0038134 ERBB2-EGFR signaling pathway | IDA PMID:11336639 Heterodimerization of the epidermal-growth-factor (EGF) rece... | ACCEPT | Summary: EGFR participates in signaling with ERBB2 in the measured heterodimer context. Reason: The original reciprocal immunoprecipitation experiments recover a small preformed EGFRβERBB2 heterodimer population, and EGF stimulates the ERBB2 Tyr1248 activation readout. The paper explicitly separates this heterodimer behavior from the high-affinity EGF-binding effect of dynamin perturbation. It does not show that every heterodimer forms only after ligand addition. Supporting Evidence: |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: The broad kinase or transferase assertion can be specified as EGFR activity. Reason: The literal InterPro, keyword, RHEA and/or ortholog arms listed in this particular source row are retained exactly. They support kinase-domain or tyrosine-phosphorylation chemistry at differing resolutions. Independent reviewed human receptor identity supports GO:0005006, which includes the receptorβs ligand-coupled tyrosine-kinase mechanism and has this original broad MF in its current closure. The refinement does not infer EGF specificity from a generic kinase domain alone or classify EGFR as a MAP kinase kinase kinase. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000002 |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | MODIFY | Summary: The broad kinase or transferase assertion can be specified as EGFR activity. Reason: The literal InterPro, keyword, RHEA and/or ortholog arms listed in this particular source row are retained exactly. They support kinase-domain or tyrosine-phosphorylation chemistry at differing resolutions. Independent reviewed human receptor identity supports GO:0005006, which includes the receptorβs ligand-coupled tyrosine-kinase mechanism and has this original broad MF in its current closure. The refinement does not infer EGF specificity from a generic kinase domain alone or classify EGFR as a MAP kinase kinase kinase. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000120 |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:15374980 A unique structure for epidermal growth factor receptor boun... | ACCEPT | Summary: Recombinant EGFR intracellular domains directly phosphorylate a tyrosine-containing peptide. Reason: The recovered author-provided original Methods measure phosphorylation of a defined ErbB peptide by purified intracellular-domain preparations, with ATP-dependent inhibition and recovery assays. This directly supports protein tyrosine kinase activity. The separate inhibitor-bound crystal uses a shorter kinase-domain construct; deposited human sequence and insect-cell expression do not make the insect host the tested protein species. Neither the fragment assay nor receptor phosphorylation in HN5 cells establishes ligand recognition by every natural EGFR product. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:17349580 Structures of lung cancer-derived EGFR mutants and inhibitor... | ACCEPT | Summary: Human EGFR kinase-domain preparations directly phosphorylate tyrosine-containing substrates. Reason: The study purified human EGFR residues696β1022, including wild type and G719S/L858R variants, after expression in Sf9 cells and tag cleavage. Its coupled ATP-consumption assay measured phosphorylation of peptide substrates, including poly(Glu,Tyr) and a receptor-tail peptide. This directly establishes protein tyrosine kinase activity at the assayed fragment level; ligand binding, intact-receptor activation and equivalence of natural products were not tested by this biochemical preparation. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:19560417 The juxtamembrane region of the EGF receptor functions as an... | ACCEPT | Summary: EGFR intracellular-domain and cellular receptor assays support intrinsic tyrosine kinase activity. Reason: The source compares sequence-checked EGFR constructs in NIH3T3, COS7 and293 cells, including full-length and intracellular-domain forms, ligand responses and a kinase-dead K721R control. The crystallized645β998 construct instead contains K721M and cannot itself be treated as an active-enzyme assay. The biochemical and cellular results support kinase activity and distinguish allosteric dimer activation from phosphorylation. Paper-specific mutation numbering and host cells are retained without claiming an authenticated current natural product. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:19563760 Mechanism for activation of the EGF receptor catalytic domai... | ACCEPT | Summary: The source directly measures EGFR tyrosine-kinase catalysis. Reason: The independent original-source assessment records phosphorylation of a tyrosine-containing peptide by purified human EGFR kinase constructs. This supports the catalytic term without treating a kinase fragment as a complete receptor. The unresolved linked erratum limits precise quantitative or mutation-specific interpretation, not an invented claim of retraction or loss of all activity. Supporting Evidence: |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:32926474 EGFR-mediated tyrosine phosphorylation of STING determines i... | ACCEPT | Summary: The STING study directly measures EGFR tyrosine-kinase activity. Reason: The original cell-free assay combines Sf9-derived commercial EGFR with purified STING-GFP and ATP. Phos-tag analysis, the STING Y245F comparison and cellular phosphosite mass spectrometry support the catalytic claim. Exact EGFR construct bounds are not supplied; this is not evidence that a natural soluble EGFR product is an autonomous kinase. Supporting Evidence: |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IBA GO_REF:0000033 | MODIFY | Summary: The broad ancestral receptor-kinase inference is sound. Human EGFR has experimental evidence for the more informative GO:0005006 epidermal growth factor receptor activity, which preserves the receptor role while specifying its ligand-receptor class. Reason: The literal PAINT IBD at PTN001230349 (GAF line 44187) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. The broad ancestral receptor-kinase inference is sound. Human EGFR has experimental evidence for the more informative GO:0005006 epidermal growth factor receptor activity, which preserves the receptor role while specifying its ligand-receptor class. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000033 |
| GO:0005515 protein binding | IPI PMID:34718348 EGF-SNX3-EGFR axis drives tumor progression and metastasis i... | UNDECIDED | Summary: The SNX3 study establishes proximity and trafficking effects, with physical binding unresolved. Reason: The SNX3 study PMID:34718348 reports TurboID-SNX3 biotinylation of endogenous EGFR in HeLa cells and EGFR-GFP in HEK293 cells, followed by neutravidin capture, together with colocalization after EGF. Its Results29β32 and Methods61 do not describe an independent native-complex coimmunoprecipitation, despite coarse anti-tag co-IP labels in two IntAct records. These positive proximity measurements and trafficking phenotypes are retained, but they do not resolve whether SNX3 physically binds EGFR. The binding assertion therefore remains undecided rather than being declared false. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35384245 Physical and functional interactome atlas of human receptor ... | UNDECIDED | Summary: SNX3 proximity is established, but physical binding remains unresolved. Reason: The literal atlas row is a BioID proximity observation. The separate SNX3 study PMID:34718348 reports TurboID-SNX3 biotinylation of endogenous EGFR in HeLa cells and EGFR-GFP in HEK293 cells, followed by neutravidin capture, together with colocalization after EGF. Its Results29β32 and Methods61 do not describe an independent native-complex coimmunoprecipitation, despite coarse anti-tag co-IP labels in two IntAct records. These positive proximity measurements and trafficking phenotypes are retained, but they do not resolve whether SNX3 physically binds EGFR. The binding assertion therefore remains undecided rather than being declared false. Supporting Evidence: |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding is an integral part of the receptor kinase mechanism. Reason: The saved target carries the mapped kinase-domain and ATP-binding-site identifiers, and its ATP-dependent tyrosine-phosphorylation chemistry makes ATP binding a mechanistic component. Preserve this source-specific positive assertion; it does not require a separate autonomous binding core or imply ATPase activity. Supporting Evidence: GO_REF:0000002 |
| GO:0016301 kinase activity | IEA GO_REF:0000107 | MODIFY | Summary: The broad kinase or transferase assertion can be specified as EGFR activity. Reason: The literal InterPro, keyword, RHEA and/or ortholog arms listed in this particular source row are retained exactly. They support kinase-domain or tyrosine-phosphorylation chemistry at differing resolutions. Independent reviewed human receptor identity supports GO:0005006, which includes the receptorβs ligand-coupled tyrosine-kinase mechanism and has this original broad MF in its current closure. The refinement does not infer EGF specificity from a generic kinase domain alone or classify EGFR as a MAP kinase kinase kinase. Proposed replacements: epidermal growth factor receptor activity Supporting Evidence: GO_REF:0000107 |
| GO:0016242 negative regulation of macroautophagy | IDA PMID:32926474 EGFR-mediated tyrosine phosphorylation of STING determines i... | KEEP AS NON CORE | Summary: EGFR activity restrains the measured STING-associated autophagy response. Reason: EGFR loss or inhibition increases LC3 lipidation after cGAMP, and STING Y245F shows corresponding trafficking and lipidation changes. The original also reports no comparable EGFR-dependent difference with Torin. The negative regulatory annotation is retained for this specific STING response, without generalizing to suppression of all macroautophagy. Supporting Evidence: |
| GO:0030182 neuron differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Neuronal differentiation is a developmental signaling context. Experimental neuron/photoreceptor-development descendants in fly Egfr support the inherited context; the exact-term query alone would have missed that grounding. Reason: The literal PAINT IBD at PTN000698827 (GAF line 45936) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Neuronal differentiation is a developmental signaling context. Experimental neuron/photoreceptor-development descendants in fly Egfr support the inherited context; the exact-term query alone would have missed that grounding. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0034165 positive regulation of toll-like receptor 9 signaling pathway | IDA PMID:40980882 TLR9 signaling requires ligand-induced phosphorylation of tw... | KEEP AS NON CORE | Summary: EGFR activity promotes the measured TLR9 signaling response. Reason: The original human-cell knockdown, knockout/rescue and inhibitor experiments support EGFR-dependent TLR9 signaling. Cellular phosphosite measurements and association support the proposed phosphorylation context, but no purified EGFRβTLR9 kinase reaction is reported. This active intracellular signaling contribution is retained without implying that the assay is driven by extracellular EGF. Supporting Evidence: |
| GO:0042059 negative regulation of epidermal growth factor receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: EGFR contributes to negative feedback through its own docking and kinase-dependent recruitment. Reason: ARBA00086227 set 1 is satisfied by three target FunFam records, but the biological justification also comes from the accepted mouse-transfer consultation. Its inspected PMID:11823423 tests receptor docking/kinase mutants and CBL/GRB2-dependent ubiquitination, internalization and signal suppression. That is active contribution to feedback, not an inference based solely on EGFR being degraded. The separate berberine donor study does not by itself prove this mechanism. Preserve the combined rule and ortholog arms with these source/construct limits. |
| GO:0043066 negative regulation of apoptotic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Anti-apoptotic signaling is a supported cellular outcome of receptor activation, retained as contextual rather than a separate defining molecular function. Reason: The literal PAINT IBD at PTN000698827 (GAF line 20006) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Anti-apoptotic signaling is a supported cellular outcome of receptor activation, retained as contextual rather than a separate defining molecular function. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0043410 positive regulation of MAPK cascade | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: MAPK activation is a supported downstream signaling output. It is retained as contextual signaling rather than a separate molecular activity. Reason: The literal PAINT IBD at PTN000698827 (GAF line 10039) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. MAPK activation is a supported downstream signaling output. It is retained as contextual signaling rather than a separate molecular activity. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE NON CORE Supporting Evidence: GO_REF:0000033 |
| GO:0050679 positive regulation of epithelial cell proliferation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Positive epithelial-proliferation regulation remains a supported tissue outcome. Reason: ARBA00089519 set 1 requires three target FunFam records and excludes Fungi; human EGFR satisfies those current literal conditions. The accepted mouse-transfer and PAINT consultations independently support the positive epithelial-proliferation outcome while retaining their primary-access limits. Keep it as non-core tissue-level regulation rather than interpreting a classifier match as proof that EGFR executes the cell cycle or that all tissues/products respond identically. Supporting Evidence: GO_REF:0000117 |
| GO:0141111 positive regulation of cGAS/STING signaling pathway | IDA PMID:32926474 EGFR-mediated tyrosine phosphorylation of STING determines i... | KEEP AS NON CORE | Summary: EGFR kinase activity promotes the IRF3 branch of STING signaling. Reason: The original combines EGFR loss/rescue, inhibitor responses and STING phosphorylation with IFN-beta and IRF3 readouts. The effect is branch-specific: NF-kappaB signaling is distinguished from the IRF3 response. EGFR contributes an active phosphorylation step in this context, without acquiring cGAS catalysis or requiring an extracellular EGF stimulus in these assays. Supporting Evidence: |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: The conserved cell-surface receptor pool is supported by the ancestral placement and independent human EGFR plasma-membrane annotations. Reason: The literal PAINT IBD at PTN001230349 (GAF line 47002) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. The conserved cell-surface receptor pool is supported by the ancestral placement and independent human EGFR plasma-membrane annotations. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: GO_REF:0000033 |
| GO:0031901 early endosome membrane | IDA PMID:40980882 TLR9 signaling requires ligand-induced phosphorylation of tw... | KEEP AS NON CORE | Summary: An engineered EGFR construct supports an early-endosomal TLR9 context. Reason: Figure4 and the original Methods localize an extracellular-domain-deleted EGFR construct with TLR9 and EEA1. This is not direct imaging of endogenous full-length receptor or a natural soluble isoform. The positive early-endosomal context is retained with the construct limitation and complementary endogenous-EGFR dependency experiments stated separately. Supporting Evidence: |
| GO:0005576 extracellular region | NAS PMID:9103388 Expression of a truncated epidermal growth factor receptor-l... | UNDECIDED | Summary: The extracellular-region assertion requires source-specific product and localization evidence. Reason: PMID:9103388 is abstract-only in the preserved cache. The abstract reports truncated EGFR-like protein expression and tumor correlations without a secretion or extracellular-localization experiment. Full text was not recovered. Preserve this NAS source context alongside the historical extracellular-space row, with uncertainty rather than a negative assertion; no exact modern isoform mapping has been established from this source. Supporting Evidence: |
| GO:0005634 nucleus | EXP PMID:17909029 The phosphoinositide kinase PIKfyve mediates epidermal growt... | KEEP AS NON CORE | Summary: A nuclear EGFR pool is detected in human bladder tumor tissue and carcinoma cells. Reason: The sourceβs complete abstract and Discussion report nuclear EGFR in a human bladder cancer tissue microarray and HB-EGF-induced nuclear trafficking in TCCSUP cells, with PIKFYVE-dependent trafficking. These positive localization observations support a context-dependent nuclear pool, consistently retained as non-core with the other nuclear-location assertions; they do not imply universal nuclear residence or sequence-specific DNA binding. The normal cache does not contain the operative Results/Methods, and the failed external route adds no assay details. Supporting Evidence: |
| GO:0005634 nucleus | EXP PMID:20674546 COPI-mediated retrograde trafficking from the Golgi to the E... | KEEP AS NON CORE | Summary: A nuclear EGFR pool is directly observed in the tested human cancer-cell systems. Reason: The original combines nuclear fractionation with mid-nuclear-plane confocal imaging in EGF-treated MDA-MB-468 cells; ARF1 mutants or BFA reduce nuclear accumulation, and gamma-COP knockdown does so in HeLa cells. Preserve the positive nuclear-location observation as a context-specific pool. The assayed EGFR was endogenous; expressed ARF1 and Golgi-marker constructs do not establish an EGFR isoform. These experiments do not independently establish nuclear transcriptional activity or the proposed final ER-to-nucleus route. Supporting Evidence: |
| GO:0005768 endosome | EXP PMID:27153536 Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a ... | ACCEPT | Summary: EGFR enters intracellular endosomal compartments in the palmitoylation study. Reason: The original human MDA-MB-231 experiments follow EGF-induced EGFR internalization and use endosomal/lysosomal markers. DHHC20 depletion changes vesicle distribution and trafficking; some peripheral vesicles lack the tested canonical markers. These results support the broad endosome annotation without assigning every observed punctum to a named endosomal subtype. Supporting Evidence: |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:27153536 Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a ... | UNDECIDED | Summary: The source-specific endoplasmic-reticulum membrane assertion remains unresolved. Reason: The recovered main original establishes EGFR surface and internal vesicular localization but does not resolve the imported ER-membrane observation. The linked supplementary PDF returned challenge HTML and could not be inspected. The annotation remains undecided; absence of an ER experiment from the recovered main text does not establish absence of an ER pool. Supporting Evidence: |
| GO:0005886 plasma membrane | EXP PMID:17182860 Activated Cdc42-associated kinase 1 is a component of EGF re... | ACCEPT | Summary: The ACK1 study detects a plasma-membrane EGFR pool before internalization. Reason: The original Results distinguish surface EGFR before EGF stimulation from subsequent vesicular localization. They also distinguish rapid association with overexpressed ACK1 at the surface from later endogenous ACK1 association. The COS7 imaging scope is preserved; these observations do not imply exclusive plasma-membrane residence or identical behavior of endogenous and overexpressed ACK1. |
| GO:0005886 plasma membrane | EXP PMID:23589287 Transforming growth factor-Ξ²1 (TGF-Ξ²1)-stimulated fibroblast... | ACCEPT | Summary: EGFR is directly detected at the plasma membrane of human lung fibroblasts. Reason: The original combines live-cell fluorescent anti-EGFR labeling, confocal imaging and fluorescence-recovery measurements in primary human lung fibroblasts and TGF-beta-differentiated myofibroblasts. It directly resolves receptor clusters at the cell membrane, with separate CD44 association and biochemical raft-fraction analyses. These results support plasma-membrane localization without requiring an exclusive raft assignment or excluding internal receptor pools. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:26918609 c-Src/Cav1-dependent activation of the EGFR by Dsg2. | ACCEPT | Summary: EGFR occupies the plasma membrane in the studied human epithelial cells. Reason: Original imaging and membrane-fraction experiments in human keratinocyte and carcinoma contexts establish EGFR at the cell surface and examine its redistribution after desmoglein-2 depletion. Detergent-resistant fractions and flotillin/caveolin markers are additional membrane-domain evidence; the STED experiment specifically images desmoglein-2 and caveolin-1 and is not misrepresented as EGFR super-resolution imaging. The supported plasma-membrane pool is nonexclusive and does not establish equivalent localization of all natural EGFR products. Supporting Evidence: |
| GO:0005886 plasma membrane | EXP PMID:27153536 Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a ... | ACCEPT | Summary: The palmitoylation study directly observes cell-surface EGFR. Reason: The original human MDA-MB-231 imaging and trafficking experiments distinguish plasma-membrane EGFR from internalized receptor after EGF. The additional NIH3T3 mutant-construct experiments are a separate system. This positive surface localization does not imply that palmitoylation confines all EGFR to the plasma membrane. Supporting Evidence: |
| GO:0005886 plasma membrane | EXP PMID:2790960 Functional independence of the epidermal growth factor recep... | ACCEPT | Summary: EGFR occupies the plasma membrane in the receptor internalization study. Reason: The complete abstract explicitly describes a membrane-bound receptor whose EGF-dependent internalization leads to down-regulation and degradation. This agrees with the curator's experimental plasma-membrane assertion and the independently supported receptor compartment. Detailed microscopy, construct and host-cell Methods were unavailable; no exclusive plasma-membrane localization is claimed. Supporting Evidence: |
| GO:0005886 plasma membrane | EXP PMID:35538033 CD82 palmitoylation site mutations at Cys5+Cys74 affect EGFR... | ACCEPT | Summary: EGFR has a measured plasma-membrane pool that changes with CD82 palmitoylation. Reason: The original uses membrane/cytoplasmic fractionation with immunoblotting and EGFR immunofluorescence in human MDA-MB-231 cells. CD82 cysteine mutants alter the distribution of EGFR between membrane and cytoplasmic pools without a corresponding change in total receptor abundance. These observations support the plasma-membrane annotation while preserving regulated intracellular trafficking. The mutations are in CD82, not EGFR, and co-immunoprecipitation is not represented as a purified binary interaction. Supporting Evidence: |
| GO:0043235 signaling receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: Membership in signaling receptor complexes is part of EGFR receptor function. This does not imply identical ligand responsiveness of every ERBB heterodimer or natural product. Reason: The literal PAINT IBD at PTN001230349 (GAF line 31496) lies on the experimentally grounded human EGFR path PTN002521387. Its ungapped sequence matches all 1,210 residues of P00533, and the path review found no same-term loss. Membership in signaling receptor complexes is part of EGFR receptor function. This does not imply identical ligand responsiveness of every ERBB heterodimer or natural product. Historical and current support sets are preserved; target self-evidence is valid descendant grounding, not circularity. The donor GOA review is distinct from a new reading of every donor paper. Propagation Review Root cause: NO FAILURE CORE Supporting Evidence: GO_REF:0000033 |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Which short natural EGFR products are secreted or retained in specific tissues, and which ligand-binding or receptor-modulatory activities are demonstrated for sequence-authenticated products?
Q: Which molecular features distinguish productive endosomal EGFR signaling from receptor pools being sorted for recycling or degradation in each physiological context?
Q: Can the DNA nicking reported for early EGFR preparations be assigned to a defined receptor construct using purified preparations and controls that exclude copurifying nucleases?
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)