Automated deep research was attempted with just deep-research-falcon human EPHA1 --fallback perplexity-lite, but the run timed out before producing a deep-research file. This review therefore uses cached GOA publications, the UniProt record, Reactome pathway records, and the PANTHER family fetch.
EPHA1 encodes ephrin type-A receptor 1, a single-pass plasma-membrane receptor tyrosine kinase. UniProt describes it as a receptor tyrosine kinase that binds membrane-bound ephrin-A ligands on adjacent cells and signals by contact-dependent forward signaling. The local PANTHER fetch places EPHA1 in PTHR46877:SF20 within the ephrin receptor tyrosine kinase family. Reactome records support the same family-level model: EPH signaling begins with ligand binding and autophosphorylation, and EPHA receptors bind EFNA ligands on closely opposed cell surfaces.
The strongest EPHA1-specific functional publication in the GOA cache is PMID:19118217, but only the abstract is cached. The abstract states that "activation of EphA1 kinase inhibits cell spreading and migration in a RhoA-ROCK-dependent manner" and that EphA1 interacts with ILK [PMID:19118217 "activation of EphA1 kinase inhibits cell spreading and migration in a RhoA-ROCK-dependent manner"; PMID:19118217 "a novel interaction between EphA1 and integrin-linked kinase (ILK)"]. This supports the core receptor-kinase, signaling, adhesion/spreading, motility, and protein-kinase-binding annotations, but the unavailable full text limits detailed assessment of assay context.
PMID:18308734, also abstract-only, supports a fibronectin-binding activity and angiogenesis-related context. The abstract states that "binding of EphA1 to fibronectin through its type I repeat played an essential role in the angiogenesis" PMID:18308734. This is a credible non-ephrin ligand interaction, but it is not the main defining receptor-tyrosine-kinase activity.
PMID:20043122, abstract-only, supports HCC-context migration and angiogenesis phenotypes. The abstract reports that EphA1 knockdown decreased Huh-7 proliferation, motility, invasion, VEGF/MMP expression, tumor outgrowth, and microvessel density [PMID:20043122 "The knockdown resulted in decreased proliferation of Huh-7 cells, as well as decreased motility and invasion capability in vitro"; PMID:20043122 "microvessel density was found to be inhibited"]. These annotations should be kept as context-dependent non-core outputs rather than the core biochemical identity of EPHA1.
PMID:16862074 is abstract-only and supports EPHA1 expression in adult human skin and nonmelanoma skin cancer, but the abstract does not verify the plasma-membrane localization detail used in GOA PMID:16862074. Plasma-membrane localization is nevertheless well supported overall by UniProt and Reactome as a single-pass cell-membrane receptor.
PMID:12775584 is abstract-only and its title/abstract concern EphA4-mediated Rho activation, not EPHA1. Per curation guidance, this is not grounds to remove the EPHA1 ephrin-receptor annotation because EPHA1 receptor activity is independently well supported, but the reference should be flagged as unverified for direct EPHA1-specific support.
For curation, accept the core ephrin receptor, transmembrane receptor tyrosine kinase, ATP/protein-tyrosine-kinase, plasma-membrane, signaling receptor complex, and ephrin receptor signaling annotations. Keep context-dependent adhesion, migration, angiogenesis, fibronectin-binding, and kinase-binding annotations as non-core where they reflect downstream or cancer-context phenotypes. Mark the stress-fiber assembly transfers as over-annotated because available cached evidence is indirect and broader RhoA/ROCK morphology terms already capture the supported mechanism better.
The second-pass audit confirmed the existing EPHA1 review and manual reference metadata. No annotation action changes were needed: EPHA1 remains curated as a plasma-membrane ephrin receptor tyrosine kinase, with adhesion, migration, angiogenesis, fibronectin-binding, and stress-fiber outputs retained as non-core or over-annotated when they represent downstream or context-specific signaling rather than the primary receptor-kinase function.