EPHA1 encodes ephrin type-A receptor 1, a single-pass plasma-membrane receptor tyrosine kinase in the Eph receptor family. It binds membrane-bound ephrin ligands on adjacent cells and signals through ligand-dependent autophosphorylation and forward signaling, coupling cell-cell contact to regulation of adhesion, spreading, migration, RhoA/ROCK-linked morphology, and context-dependent angiogenic or tumor cell behaviors. EPHA1 contains an extracellular ephrin ligand-binding region, a single transmembrane segment, an intracellular tyrosine kinase domain, and a SAM domain.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0043235 signaling receptor complex | IBA GO_REF:0000033 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as a core receptor-complex annotation. Eph signaling requires ligand-bound receptor complexes at opposed cell membranes, and Reactome describes EPHA/EFNA binding, dimerization, tetramerization, and autophosphorylation events. |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0004714 transmembrane receptor protein tyrosine kinase activity | IEA GO_REF:0000003 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0005003 ephrin receptor activity | IEA GO_REF:0000120 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0005005 transmembrane-ephrin receptor activity | IEA GO_REF:0000117 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0016020 membrane | IEA GO_REF:0000002 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0030155 regulation of cell adhesion | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as a biologically supported but context-dependent downstream output. EPHA1 activation regulates morphology, adhesion, and motility through ILK/RhoA/ROCK, while HCC and fibronectin studies support angiogenesis and fibronectin-related phenotypes. These outputs are important but secondary to the defining ephrin receptor tyrosine kinase activity. |
| GO:0048013 ephrin receptor signaling pathway | IEA GO_REF:0000120 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0045766 positive regulation of angiogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as non-core. Angiogenesis evidence comes from cancer/knockdown or fibronectin-ligand contexts (PMID:20043122, PMID:18308734), making it a relevant phenotype rather than the core molecular role. |
| GO:0051496 positive regulation of stress fiber assembly | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Stress-fiber assembly is an indirect transferred downstream term for EPHA1. Reason: Mark as over-annotated because the cached evidence for stress-fiber assembly is indirect/transfer-based, and the more directly supported EPHA1 biology is receptor tyrosine kinase signaling through ILK/RhoA/ROCK with effects on spreading and migration. Broader morphology/motility annotations capture the evidence better. |
| GO:0005003 ephrin receptor activity | IDA PMID:12775584 EphA4-mediated Rho activation via Vsm-RhoGEF expressed speci... | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IDA PMID:19118217 EphA1 interacts with integrin-linked kinase and regulates ce... | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0001968 fibronectin binding | IDA PMID:18308734 Fibronectin type I repeat is a nonactivating ligand for EphA... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as non-core. PMID:18308734 supports fibronectin binding as a nonactivating ligand interaction involved in angiogenesis, but canonical ephrin receptor/tyrosine kinase activity remains the defining molecular function of EPHA1. |
| GO:0045766 positive regulation of angiogenesis | ISS PMID:18308734 Fibronectin type I repeat is a nonactivating ligand for EphA... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as non-core. Angiogenesis evidence comes from cancer/knockdown or fibronectin-ligand contexts (PMID:20043122, PMID:18308734), making it a relevant phenotype rather than the core molecular role. |
| GO:0005886 plasma membrane | IDA PMID:16862074 Expression profile of Eph receptors and ephrin ligands in hu... | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928578 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928604 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928607 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928628 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928642 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928651 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-4093327 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928591 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928597 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928646 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-480509 | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0051496 positive regulation of stress fiber assembly | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Stress-fiber assembly is an indirect transferred downstream term for EPHA1. Reason: Mark as over-annotated because the cached evidence for stress-fiber assembly is indirect/transfer-based, and the more directly supported EPHA1 biology is receptor tyrosine kinase signaling through ILK/RhoA/ROCK with effects on spreading and migration. Broader morphology/motility annotations capture the evidence better. |
| GO:0001954 positive regulation of cell-matrix adhesion | IDA PMID:19118217 EphA1 interacts with integrin-linked kinase and regulates ce... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as a biologically supported but context-dependent downstream output. EPHA1 activation regulates morphology, adhesion, and motility through ILK/RhoA/ROCK, while HCC and fibronectin studies support angiogenesis and fibronectin-related phenotypes. These outputs are important but secondary to the defining ephrin receptor tyrosine kinase activity. |
| GO:0005005 transmembrane-ephrin receptor activity | IDA PMID:19118217 EphA1 interacts with integrin-linked kinase and regulates ce... | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept as part of the core EPHA1 functional profile. UniProt, PANTHER, Reactome, and EPHA1-specific abstracts support EPHA1 as a single-pass plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands, autophosphorylates, and mediates cell-surface receptor protein tyrosine kinase/ephrin receptor signaling. |
| GO:0005886 plasma membrane | IDA PMID:19118217 EphA1 interacts with integrin-linked kinase and regulates ce... | ACCEPT | Summary: EPHA1 is a plasma-membrane Eph receptor tyrosine kinase that binds ephrin ligands and signals through ligand-dependent kinase activation/autophosphorylation. Reason: Accept plasma-membrane localization because EPHA1 is a single-pass Eph receptor at the cell membrane; this is supported by UniProt and Reactome, and is consistent with the curated IDA/TAS plasma-membrane annotations. The PMID:16862074 cache is abstract-only, so that specific localization paper cannot be fully re-reviewed here. |
| GO:0019901 protein kinase binding | IPI PMID:19118217 EphA1 interacts with integrin-linked kinase and regulates ce... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as non-core. PMID:19118217 reports interaction with the protein kinases ILK and PTK2/FAK1, but protein kinase binding is an interaction mechanism downstream of ligand-stimulated EPHA1 rather than the primary receptor activity. |
| GO:0030335 positive regulation of cell migration | IMP PMID:20043122 EphA1 receptor silencing by small interfering RNA has antian... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as a biologically supported but context-dependent downstream output. EPHA1 activation regulates morphology, adhesion, and motility through ILK/RhoA/ROCK, while HCC and fibronectin studies support angiogenesis and fibronectin-related phenotypes. These outputs are important but secondary to the defining ephrin receptor tyrosine kinase activity. |
| GO:0030336 negative regulation of cell migration | IDA PMID:19118217 EphA1 interacts with integrin-linked kinase and regulates ce... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as a biologically supported but context-dependent downstream output. EPHA1 activation regulates morphology, adhesion, and motility through ILK/RhoA/ROCK, while HCC and fibronectin studies support angiogenesis and fibronectin-related phenotypes. These outputs are important but secondary to the defining ephrin receptor tyrosine kinase activity. |
| GO:0034446 substrate adhesion-dependent cell spreading | IDA PMID:19118217 EphA1 interacts with integrin-linked kinase and regulates ce... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as a biologically supported but context-dependent downstream output. EPHA1 activation regulates morphology, adhesion, and motility through ILK/RhoA/ROCK, while HCC and fibronectin studies support angiogenesis and fibronectin-related phenotypes. These outputs are important but secondary to the defining ephrin receptor tyrosine kinase activity. |
| GO:0045766 positive regulation of angiogenesis | IMP PMID:20043122 EphA1 receptor silencing by small interfering RNA has antian... | KEEP AS NON CORE | Summary: This annotation describes a context-dependent downstream adhesion, migration, angiogenesis, or interaction output of EPHA1 signaling rather than the core receptor-kinase activity. Reason: Keep as non-core. Angiogenesis evidence comes from cancer/knockdown or fibronectin-ligand contexts (PMID:20043122, PMID:18308734), making it a relevant phenotype rather than the core molecular role. |
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Download this section (compressed HTML)Q: Which EPHA1 downstream outputs are conserved physiological functions versus cancer- or cell-line-specific phenotypes?
Q: Does EPHA1 have Alzheimer-relevant roles in brain vascular, epithelial/barrier, immune, or glial cell contexts, or is its disease association indirect?
Q: Should the PMID:12775584 annotation be rechecked against full text or source curation notes, since the cached abstract is EphA4-focused?
Experiment: Stimulate endogenous EPHA1 with ephrin-A1 in epithelial, endothelial, and myeloid/glial models, then measure autophosphorylation, ILK/FAK recruitment, RhoA activity, stress-fiber morphology, adhesion, spreading, and migration.
Hypothesis: EPHA1 regulates adhesion and motility through ligand-dependent ILK/RhoA/ROCK signaling in a cell-type-specific manner.
Type: ligand-stimulation signaling assay
Experiment: Perturb EPHA1 in human iPSC-derived endothelial, pericyte, astrocyte, and microglial co-culture systems and assay barrier integrity, cell-cell repulsion/adhesion, inflammatory signaling, and amyloid-related stress responses.
Hypothesis: EPHA1 Alzheimer relevance depends on vascular or barrier-cell signaling rather than a neuron-intrinsic core function.
Type: disease-context functional assay
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