Epha2
entrez
13836
canonical
uniprot
Q03145
canonical
ensembl
ENSMUSG00000006445
resolver
ensp
ENSMUSP00000006614
resolver
enst
ENSMUST00000006614
resolver
genesymbol
Epha2
resolver
genesymbol_syn
Eck
resolver
genesymbol_syn
Myk2
resolver
genesymbol_syn
Sek2
resolver
uniprot
Q3UNI2
resolver
uniprot
Q60633
resolver
uniprot
Q62212
resolver
uniprot_entry
EPHA2_MOUSE
resolver
uniprot_sec
Q3UNI2
resolver
uniprot_sec
Q60633
resolver
uniprot_sec
Q62212
resolver
amino_acid_sequence
MELRAVGFCLALLWGCALAAAAAQGKEVVLLDFAAMKGELGWLTHPYGKGWDLMQNIMDDMPIYMYSVCNVVSGDQDNWLRTNWVYREEAERIFIELKFTVRDCNSFPGGASSCKETFNLYYAESDVDYGTNFQKRQFTKIDTIAPDEITVSSDFEARNVKLNVEERMVGPLTRKGFYLAFQDIGACVALLSVRVYYKKCPEMLQSLARFPETIAVAVSDTQPLATVAGTCVDHAVVPYGGEGPLMHCTVDGEWLVPIGQCLCQEGYEKVEDACRACSPGFFKSEASESPCLECPEHTLPSTEGATSCQCEEGYFRAPEDPLSMSCTRPPSAPNYLTAIGMGAKVELRWTAPKDTGGRQDIVYSVTCEQCWPESGECGPCEASVRYSEPPHALTRTSVTVSDLEPHMNYTFAVEARNGVSGLVTSRSFRTASVSINQTEPPKVRLEDRSTTSLSVTWSIPVSQQSRVWKYEVTYRKKGDANSYNVRRTEGFSVTLDDLAPDTTYLVQVQALTQEGQGAGSKVHEFQTLSTEGSANMAVIGGVAVGVVLLLVLAGVGLFIHRRRRNLRARQSSEDVRFSKSEQLKPLKTYVDPHTYEDPNQAVLKFTTEIHPSCVARQKVIGAGEFGEVYKGTLKASSGKKEIPVAIKTLKAGYTEKQRVDFLSEASIMGQFSHHNIIRLEGVVSKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIASGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSYGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERSRRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSGSEGVPFRTVSEWLESIKMQQYTEHFMVAGYTAIEKVVQMSNEDIKRIGVRLPGHQKRIAYSLLGLKDQVNTVGIPI
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
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 (PubMed:29749928). Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 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. {ECO:0000269|PubMed:15054110, ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:16849550, ECO:0000269|PubMed:18387945, ECO:0000269|PubMed:18948590, ECO:0000269|PubMed:19299512, ECO:0000269|PubMed:19321667, ECO:0000269|PubMed:29749928}.
uniprot
proteins
mass_dalton
108852
uniprot
proteins
mutagenesis
MUTAGEN 589; /note="Y->E: No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-595."; /evidence="ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:18387945"; MUTAGEN 589; /note="Y->F: Inhibits EFNA1-induced vascular assembly and kinase activity."; /evidence="ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:18387945"; MUTAGEN 595; /note="Y->E: No significant effect on kinase activity and loss of binding to VAV2 and VAV3. Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells, no significant effect on kinase activity, significant reduction in phosphorylation and binding to VAV3; when associated with E-589."; /evidence="ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:18387945"; MUTAGEN 595; /note="Y->F: Inhibits EFNA1-induced vascular assembly and abolishes kinase activity."; /evidence="ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:18387945"; MUTAGEN 736; /note="Y->F: Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. No significant effect on kinase activity. Loss of binding to PI3-kinase p85 subunit."; /evidence="ECO:0000269|PubMed:18387945"; MUTAGEN 740; /note="D->N: Loss of kinase activity and binding to VAV3."; /evidence="ECO:0000269|PubMed:16782872"; MUTAGEN 773; /note="Y->F: No significant effect on kinase activity. Significant reduction in phosphorylation."; /evidence="ECO:0000269|PubMed:18387945"; MUTAGEN 918; /note="K->A: Strongly reduced binding affinity for INPPL1 SAM domain."; /evidence="ECO:0000269|PubMed:29749928"; MUTAGEN 931; /note="Y->F: Inhibits EFNA1-induced vascular assembly and RAC1 activation in endothelial cells. Inhibits kinase activity. Loss of binding to VAV3 and PI3-kinase p85 subunit."; /evidence="ECO:0000269|PubMed:18387945"; MUTAGEN 957; /note="K->A: Strongly reduced binding affinity for INPPL1 SAM domain."; /evidence="ECO:0000269|PubMed:29749928"; MUTAGEN 958; /note="R->C,K: Abolishes interaction with INPPL1 SAM domain."; /evidence="ECO:0000269|PubMed:29749928
uniprot
proteins
post_translational_modification
PTM: Autophosphorylates. Phosphorylated at Ser-898 by PKB; serum-induced phosphorylation which targets EPHA2 to the cell leading edge and stimulates cell migration. Phosphorylation by PKB is inhibited by EFNA1-activated EPHA2 which regulates PKB activity via a reciprocal regulatory loop. Phosphorylated on tyrosine upon binding and activation by EFNA1. Phosphorylated residues Tyr-589 and Tyr-595 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-736 and Tyr-931 are required for binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These phosphorylated residues are critical for recruitment of VAV2 and VAV3 and PI3-kinase p85 subunit which transduce downstream signaling to activate RAC1 GTPase and cell migration. Dephosphorylation of Tyr-931 by PTPRF prevents the interaction of EPHA2 with NCK1. Phosphorylated at Ser-898 in response to TNF by RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration. Phosphorylated at Ser-898 by PKA; blocks cell retraction induced by EPHA2 kinase activity. Dephosphorylated by ACP1. {ECO:0000250|UniProtKB:P29317, ECO:0000269|PubMed:18387945}.; PTM: Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by the HSP90 chaperone and regulates the receptor stability and activity through proteasomal degradation. ANKS1A prevents ubiquitination and degradation. {ECO:0000269|PubMed:20100865}.
uniprot
proteins
protein_family
Ephrin receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
11287184
uniprot
proteins
pubmed
1281307
uniprot
proteins
pubmed
15054110
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16782872
uniprot
proteins
pubmed
16849550
uniprot
proteins
pubmed
18387945
uniprot
proteins
pubmed
18948590
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19299512
uniprot
proteins
pubmed
19321667
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19656770
uniprot
proteins
pubmed
20100865
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27446912
uniprot
proteins
pubmed
29749928
uniprot
proteins
pubmed
7543898
uniprot
proteins
pubmed
7918100
uniprot
proteins
pubmed
7947319
uniprot
proteins
pubmed
8183555
uniprot
proteins
sequence_length
977
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P29317}. Note=Present at regions of cell-cell contacts but also at the leading edge of migrating cells. Relocates from the plasma membrane to the cytoplasmic and perinuclear regions in cancer cells. {ECO:0000250|UniProtKB:P29317}.
uniprot
proteins
transmembrane_region
TRANSMEM 539..559; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins