Names & Taxonomy

Uniprot ID:
P29317
Entry Name:
EPHA2_HUMAN
Status:
reviewed
Protein Names:
Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK)
Gene Names:
EPHA2 ECK
Gene Names Primary:
EPHA2
Organism:
Homo sapiens (Human)

Structure

Length:
976
Sequence:
MELQAARACFALLWGCALAAAAAAQGKEVVLLDFAAAGGELGWLTHPYGKGWDLMQNIMNDMPIYMYSVCNVMSGDQDNWLRTNWVYRGEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDLDYGTNFQKRLFTKIDTIAPDEITVSSDFEARHVKLNVEERSVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPELLQGLAHFPETIAGSDAPSLATVAGTCVDHAVVPPGGEEPRMHCAVDGEWLVPIGQCLCQAGYEKVEDACQACSPGFFKFEASESPCLECPEHTLPSPEGATSCECEEGFFRAPQDPASMPCTRPPSAPHYLTAVGMGAKVELRWTPPQDSGGREDIVYSVTCEQCWPESGECGPCEASVRYSEPPHGLTRTSVTVSDLEPHMNYTFTVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEGRSTTSLSVSWSIPPPQQSRVWKYEVTYRKKGDSNSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSPEGSGNLAVIGGVAVGVVLLLVLAGVGFFIHRRRKNQRARQSPEDVYFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMAAGYTAIEKVVQMTNDDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Cell membrane

Function

Function:
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis.
Catalytic Activity:
ATP + a -L-tyrosine = ADP + a -L-tyrosine phosphate.
Active Site:
ACT_SITE 739 739 Proton acceptor.
Cross Reference Drug Bank:
DB01254 DB08896
Gene Ontology Go:
cell surface
focal adhesion
integral component of plasma membrane
intracellular
lamellipodium membrane
leading edge membrane
plasma membrane
ruffle membrane
ATP binding
ephrin receptor activity
transmembrane receptor protein tyrosine kinase activity
activation of GTPase activity
angiogenesis
axial mesoderm formation
axon guidance
bone remodeling
branching involved in mammary gland duct morphogenesis
cell adhesion
cell chemotaxis
cell migration
ephrin receptor signaling pathway
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 protein kinase B signaling
neural tube development
notochord cell development
notochord formation
osteoblast differentiation
osteoclast differentiation
peptidyl-tyrosine phosphorylation
positive regulation of establishment of protein localization to plasma membrane
post-anal tail morphogenesis
protein kinase B signaling
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 process
Gene Ontology Biological Process:
activation of GTPase activity
angiogenesis
axial mesoderm formation
axon guidance
bone remodeling
branching involved in mammary gland duct morphogenesis
cell adhesion
cell chemotaxis
cell migration
ephrin receptor signaling pathway
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 protein kinase B signaling
neural tube development
notochord cell development
notochord formation
osteoblast differentiation
osteoclast differentiation
peptidyl-tyrosine phosphorylation
positive regulation of establishment of protein localization to plasma membrane
post-anal tail morphogenesis
protein kinase B signaling
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 process
Gene Ontology Molecular Function:
ATP binding
ephrin receptor activity
transmembrane receptor protein tyrosine kinase activity
Gene Ontology Cellular Component:
cell surface
focal adhesion
integral component of plasma membrane
intracellular
lamellipodium membrane
leading edge membrane
plasma membrane
ruffle membrane
Keywords:
3D-structure
ATP-binding
Alternative splicing
Angiogenesis
Apoptosis
Cataract
Cell adhesion
Cell junction
Cell membrane
Cell projection
Complete proteome
Differentiation
Disease mutation
Disulfide bond
Glycoprotein
Host-virus interaction
Kinase
Membrane
Nucleotide-binding
Phosphoprotein
Polymorphism
Receptor
Reference proteome
Repeat
Signal
Transferase
Transmembrane
Transmembrane helix
Tyrosine-protein kinase
Ubl conjugation
Interacts With:
P20827; Q15375; P08238; Q05397

Publication

PubMed ID:
2174105 18593464 16710414 15489334 9267020 10655584 11280802 12167657 16236711 17332925 17135240 18339848 18691976 18794797 18669648 19573808 19159218 19567782 19369195 20679435 20861311 20068231 21269460 22332920 22635007 23358419 23936024 12467573 19525919 20505120 17344846 19005574 19306328 19649315 22570727