EphA2 a receptor tyrosine kinase. Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A3, -A4 AND -A5. The Eph receptor tyrosine kinase family, the largest in the tyrosine kinase group, has fourteen members. They bind membrane-anchored ligands, ephrins, at sites of cell-cell contact, regulating the repulsion and adhesion of cells that underlie the establishment, maintenance, and remodeling of patterns of cellular organization. Eph signals are particularly important in regulating cell adhesion and cell migration during development, axon guidance, homeostasis and disease. EphA receptors bind to GPI-anchored ephrin-A ligands, while EphB receptors bind to ephrin-B proteins that have a transmembrane and cytoplasmic domain. Interactions between EphB receptor kinases and ephrin-B proteins transduce signals bidirectionally, signaling to both interacting cell types. Eph receptors and ephrins also regulate the adhesion of endothelial cells and are required for the remodeling of blood vessels. Overexpressed in many cancers including aggressive ovarian, cervical and breast carcinomas, and lung cancer. Expression correlates with degree of angiogenesis, metastasis and xenograft tumor growth. Soluble receptor inhibits tumor growth and angiogenesis in mice. Note: This description may include information from UniProtKB.
Protein type: EC; Eph family; Kinase, protein; Membrane protein, integral; Protein kinase, TK; Protein kinase, tyrosine (receptor); TK group
Chromosomal Location of Human Ortholog: 1p36.13
Cellular Component:  cell surface; focal adhesion; integral component of plasma membrane; lamellipodium; lamellipodium membrane; leading edge membrane; plasma membrane; ruffle membrane; tight junction
Molecular Function:  ATP binding; protein binding; transmembrane receptor protein tyrosine kinase activity; virus receptor activity
Biological Process:  activation of GTPase activity; axial mesoderm formation; blood vessel endothelial cell proliferation involved in sprouting angiogenesis; bone remodeling; branching involved in mammary gland duct morphogenesis; cAMP metabolic process; cell adhesion; cell chemotaxis; cell migration; cell motility; defense response to Gram-positive bacterium; ephrin receptor signaling pathway; inflammatory response; intrinsic apoptotic signaling pathway in response to DNA damage; keratinocyte differentiation; lens fiber cell morphogenesis; mammary gland epithelial cell proliferation; multicellular organism development; negative regulation of angiogenesis; negative regulation of chemokine production; negative regulation of lymphangiogenesis; negative regulation of protein kinase B signaling; neural tube development; notochord cell development; notochord formation; osteoblast differentiation; osteoclast differentiation; peptidyl-tyrosine phosphorylation; pericyte cell differentiation; positive regulation of bicellular tight junction assembly; positive regulation of protein localization to plasma membrane; post-anal tail morphogenesis; protein kinase B signaling; protein localization to plasma membrane; regulation of angiogenesis; regulation of blood vessel endothelial cell migration; regulation of cell adhesion mediated by integrin; regulation of ERK1 and ERK2 cascade; regulation of lamellipodium assembly; response to growth factor; skeletal system development; vasculogenesis; viral entry into host cell
Disease: Cataract 6, Multiple Types
Reference #:  P29317 (UniProtKB)
Alt. Names/Synonyms: ARCC2; ECK; EPH receptor A2; EPHA2; ephrin receptor EphA2; Ephrin type-A receptor 2; Epithelial cell kinase; epithelial cell receptor protein tyrosine kinase; protein tyrosine kinase; soluble EPHA2 variant 1; Tyrosine-protein kinase receptor ECK
Gene Symbols: EPHA2
Molecular weight: 108,266 Da
Basal Isoelectric point: 5.86  Predict pI for various phosphorylation states
CST Pathways:  Tyrosine Kinases & Substrates
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

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