Atlas of Genetics and Cytogenetics in Oncology and Haematology

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EPHA3 (EPH receptor A3)


Other namesEK4
LocusID (NCBI) 2042
Atlas_Id 40463
Location 3p11.1
Location_base_pair Starts at 89156674 and ends at 89531284 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order (tel) C3orf38 (ENSG00000179021) ->, 949,562bp, EPHA3 (374,609bp) ->, 720,071bp, <- AC139337.5 (ENSG00000189002) (cen)
  Figure 1: Chromosomal location of EPHA3 (based on Ensembl Homo sapiens version 53.36o (NCBI36)).
Figure 2: Genomic neighbourhood of EPHA3 (based on Ensembl Homo sapiens version 53.36o (NCBI36)).
Fusion genes
(updated 2015)
LCLAT1 (2p23.1) / EPHA3 (3p11.1)
Note EPHA3 is flanked by two gene deserts.


Note EPHA3 spans the human tile path clones CTD-2532M17, RP11-784B9 and RP11-547K2.
  Figure 3: Genomic organisation of EPHA3.
Description EPHA3 consists of 17 exons and 16 introns and spans 375kb of genomic DNA. It is the second largest of the EPH genes after EPHA6.
Transcription Two alternatively spliced transcript variants have been described (NM_005233.5, a 5,807 nucleotide mRNA and NM_182644.2, a 2,684 nucleotide mRNA). The shorter transcript results in truncation within the extracellular domain of EphA3 and is predicted to produce a soluble protein. The 5' end of EPHA3 is associated with a CpG island, a feature common to all EPH genes. The EPHA3 promoter also lacks a TATA box and transcription initiates from multiple start sites.
Pseudogene None identified.


Note The Eph receptors constitute the largest of the 20 subfamilies of human receptor tyrosine kinases. The founding member of this group was isolated originally from an erythropoietin producing hepatoma cell line.
  Figure 4: Domain organisation of EphA3.
Description The EPHA3 gene encodes a 983 amino acid protein with a calculated molecular weight of 110.1kDa and an isoelectric point of 6.7302. Amino acids 1-20 constitute a signal peptide. The predicted molecular mass of the translated protein minus the signal peptide is 92.8kDa. The 521 amino acid extracellular domain contains five potential sites for N-glycosylation such that EphA3 is typically detected as a 135kDa glycoprotein. This mature isoform of EphA3 is a single-pass transmembrane receptor tyrosine kinase. Eph receptors have a conserved domain structure: At the N-terminus is a ≈ 174 amino acid ligand binding domain, followed by a ≈114 amino acid cysteine-rich domain subdivided into complement control protein (CCP, or sushi) and EGF-like domains and two membrane proximal fibronectin type III repeats. Amino acids 21-376 of the extracellular domain are rich in cysteine residues. The intracellular domain contains the tyrosine kinase domain and a sterile alpha motif. EphA3 lacks a PDZ domain interacting motif present in EphA7, EphB2, EphB3, EphB5 and EphB6. Activation of the EphA3 receptor tyrosine kinase domain is associated with two tyrosine residues in the juxtamembrane region (Y596, Y602) that are sites of autophosphorylation and interact with the kinase domain to modulate its activity.
EphA3 belongs to an evolutionarily ancient subfamily of receptor tyrosine kinases with members being present in sponges, worms and fruit flies. The expansion in the number of Eph receptor-encoding genes along with genes encoding their ligands, the ephrins (Eph receptor interacting proteins), is proposed to have contributed to the increase in complexity of the bilaterian body plan. Genes encoding EphA3 are found in the genomes of representative members of at least five of the seven classes of vertebrates including bony fish (zebrafish, pufferfish, medaka), amphibians (African clawed frog), reptiles (green anole lizard), birds (chicken) and mammals (platypus, possum, human).
Fourteen Eph receptors have been identified in vertebrates. These are subdivided into either EphA (EphA1, EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, EphA8, EphA10) or EphB (EphB1, EphB2, EphB3, EphB4, EphB6) subclasses which differ primarily in the structure of their ligand binding domains. EphA receptors also exhibit greater affinity for binding GPI-linked ephrin-A ligands while EphB receptors bind transmembrane ephrin-B ligands. While interactions are somewhat promiscuous, and some cross-class binding occurs, each Eph receptor displays distinct affinity for the different ephrin ligands. The high affinity ligands for EphA3 are ephrin-A2 and ephrin-A5. EphA3 also binds ephrin-A3 and ephrin-A4 with lower affinity.
Eph-ephrin binding involves contact between cells. Upon binding, receptor-ligand dimers form heterotetramers, which further assemble into higher order signalling clusters. Several moieties in the EphA3 receptor extracellular region mediate ephrin binding. A high-affinity binding site in the N-terminal ephrin binding domain mediates intercellular Eph-ephrin interaction. Structural studies show the interaction between ephrin-A5 and EphA3 is slightly tilted relative to its binding to EphA2, resulting in a greater interaction surface . Mutation studies show two additional lower-affinity ephrin-binding sites, one in the ephrin-binding domain and the other in the cysteine-rich region, are involved in clustering of the EphA3-ephrin-A5 complex. Receptor clustering is further facilitated by receptor-receptor interactions within the ligand-binding domain and the adjacent cysteine-rich domain , which can also lead to heterologous clustering with different Eph subtypes .
Following ephrin-A5-mediated EphA3 receptor clustering, intracellular signalling by EphA3 receptors is initiated by autophosphorylation of three defined tyrosine residues, two in the highly conserved juxtamembrane region and the third in the activation loop of the kinase domain (Y779). Rapid reorganisation of the actin and myosin cytoskeleton follows, leading to retraction of cellular protrusions, membrane blebbing and cell detachment, following association of the adaptor protein CrkII with tyrosine phosphorylated EphA3 and activation of RhoA signalling.
Such Eph-ephrin interaction triggers bidirectional signalling, that is signalling events within both Eph- and ephrin-bearing cells, an unusual phenomenon for receptor tyrosine kinases, most of which interact with soluble ligands. Subsequently, depending on the cellular context (including the identity of the interacting Eph-ephrin receptor-ligand pairs, their relative levels on interacting cells, the presence of additional Ephs and ephrins and their alternative isoforms, and the net effect of interaction with additional signalling pathways) this either results in repulsion or promotes adhesion of the interacting cells.
Cellular repulsion and the termination of Eph-ephrin signalling require disruption of the receptor-ligand complex. This is brought about either by enzymatic cleavage of the tethered ephrin ligand or by trans endocytosis of Eph-ephrin complexes. EphA3-ephrin-A receptor-ligand complexes are disrupted following receptor-ligand binding when ADAM10 (a disintegrin and metalloprotease 10), cleaves ephrin cleaves ephrin, to allow cells to separate. ADAM10 association via its substrate recognition motif, and cleavage of ephrin, are dependent on ephrin/EphA3 binding and on EphA3 kinase activation. The post-cleavage ephrin-A5-EphA3 complex is then endocytosed by the EphA3-expressing cell.
While cellular repulsion is often the outcome of Eph-ephrin interaction, in some circumstances adhesion may persist, particularly when there is low Eph kinase activity. For example, ADAM10 has been observed not to cleave ephrin-A5 following EphA3-ephrin-A5 interaction involving LK63 cells in which high intracellular protein tyrosine phosphatase activity also appears to counter ephrin-A5 stimulated phosphorylation of EphA3, holding the receptor in an inactive, unphosphorylated state. The phosphatase PTP1B is known to directly regulate EphA3 activity, and its overexpression inhibits receptor endocytosis at cell-cell contacts . Another mechanism that may favour stable cell-cell adhesion involves truncated Eph receptor isoforms acting in a dominant negative manner. While activation of full length EphA7 by ephrin-A5 results in cellular repulsion, ephrin-A5-induced phosphorylation of EphA7 is inhibited by expression of two EphA7 splice variants with truncated kinase domains, which act in a dominant negative manner, and adhesion results. A splice variant of EPHA3 also has been reported, truncated before the transmembrane domain, and predicted to give rise to a soluble isoform of EphA3, the function of which has not been established. In addition, a number of EphA3 mutations have been described in various cancers (see below), at least some of which inhibit activity and cell-surface localisation of the receptor , and can act as dominant negative mutants to inhibit activity of Wt receptor .
While important details of EphA3 signalling have been determined, more complete understanding of EphA3 activity will require knowledge of the full complement of EphA3 interacting proteins. Substrates that are targets for the tyrosine kinase activity of EphA3 have yet to be defined and potential mediators or modulators of EphA3 signalling output such as Src family kinases, additional phosphotyrosine binding adaptors, SAM domain interacting factors, interaction with other receptor kinases and crosstalk with other signalling pathways, and the regulatory role of phosphatases all remain to be explored. Based on the range of interacting proteins identified for other Eph receptors (some common to more than one Eph, others apparently unique to individual Ephs) additional effectors of EphA3 signalling output are likely.
Expression EphA3 was first identified as an antigen expressed at high levels (10,000-20,000 copies per cell) on the surface of the LK63 pre-B cell acute lymphoblastic leukaemia cell line. It also was found to be expressed by JM, HSB-2 and MOLT-4 T-cell leukaemic cell lines, in CD28-stimulated Jurkat cells, and in 16 of 42 cases of primary T-cell lymphoma (but not normal peripheral T lymphocytes nor in any subset of thymus-derived developing T cells). It is also present in patients with hematologic malignancies, including AML, CML, MDS, MPN and Multiple Myeloma, and in various solid tumours (see below)
EphA3 expression has been shown to be most abundant during vertebrate development, where it is highly regulated both temporally and spatially. Prominent EphA3 expression occurs in the neural system, including the retinal ganglion cells of the embryonic retina in a graded distribution from anterior/nasal (lowest) to posterior/temporal (highest); the cerebrum, thalamus, striatum, olfactory bulb, anterior commissure, and corpus callosum of the forebrain; and the medial motor column ventral motor neurons of the spinal cord; and extraneurally by mesodermally-derived tissues including the paraxial musculature, tongue musculature, submucosa of the soft palate, capsule of the submandibular gland, cortical rim of bone, thymic septae, media of the pharynx, trachea, great vessels, small intestine and portal vein, cardiac valves, and the renal medulla. In adult tissues EphA3 expression is more restricted and detected at significantly lower levels than during early development. However it is expressed on mesenchymal stromal progenitor cells (MSCs) during neovascularisation of the regenerating endometrium, with its expression regulated by hypoxia. Similarly EphA3 is expressed on MSCs recruited from the bone-marrow and contributing to the vasculature and supporting stromal tissue of various solid cancers . It is also over-expressed on progenitor cells in gliomas. In these instances EphA3 in tumours is largely inactive, and activation with an agonistic antibody inhibits tumour growth.
Loss of EphA3 expression is also reported in cancer. EPHA3 gene copy number and/or expression levels were decreased in lung cancers (157 of 371 primary lung adenocarcinomas), and also in esophageal squamous cell carcinoma (ESCC). Silencing of EPHA3 expression by DNA hypermethylation occurs in leukaemia , and in colorectal tumours carrying a BRAF mutation (V600E). Somatic mutations identified in the 3' untranslated region of EPHA3 may also disrupt miRNA target sites, thereby altering its expression .
Localisation Isoform 1: Cell membrane; single-pass type I membrane protein.
Isoform 2: Secreted.
Function Eph receptors modulate cell shape and movement through reorganisation of the cytoskeleton and changes in cell-cell and cell-substrate adhesion, and are involved in many cellular migration, sorting (tissue patterning) and guidance events, most often during development, and in particular involving the nervous system. There is evidence too that Eph receptor signalling influences cell proliferation and cell-fate determination and growing recognition that Eph receptors function in adult tissue homeostasis.
EphA3 is thought to play a role in retinotectal mapping, the tightly patterned projection of retinal ganglion cell axons from the retina to the optic tectum (or superior colliculus in mammals). In chicks, posterior retinal ganglion axons expressing highest levels of EphA3 project to the anterior tectum where the graded expression of ephrin-A2 and ephrin-A5 is lowest and are excluded from projecting more posteriorly where ephrin-A2/A5 expression is highest. More direct evidence of non-redundant function for EphA3 has come from phenotypic analysis of EphA3 knockout mice. Approximately 70-75% of EphA3 null mice die within 48 hours of birth with post-mortem evidence of pulmonary oedema secondary to cardiac failure. These mice exhibit hypoplastic atrioventricular endocardial cushions and subsequent atrioventricular valve and atrial membranous septal defects, with endocardial cushion explants from these mice giving rise to fewer migrating cells arising from epithelial to mesenchymal transformation. Expression of EphA3 in the spinal cord appears to be redundant as axial muscle targeting by medial motor column motor axons and the organisation of the motor neuron columns is not altered. EphA4 is the only other EphA receptor also expressed by developing spinal cord motor neurons and in mice lacking EphA3 and EphA4 these receptors together repel axial motor axons from neighbouring ephrin-A-expressing sensory axons, inhibiting intermingling of motor and sensory axons and preventing mis-projection of motor axons into the dorsal root ganglia. In contrast to the chick, EphA3 is not expressed by mouse retinal ganglion cells. Instead the closely related receptors EphA5 and EphA6 (see homology below) are expressed in a low nasal to high temporal gradient. However, if EphA3 is ectopically expressed in retinal ganglion cells in mice these axons project to more rostral positions in the superior colliculus.
A function for soluble EphA3 has not been reported although potentially this isoform might play a role in promoting cell adhesion (see above) or act as a tumour suppressor protein (see below).
Homology Phylogenetic tree for the Eph receptors. Amino acid sequences used for this compilation were EphA1 (NP_005223), EphA2 (NM_004431), EphA3 (NP_005224), EphA4 (NP_004429), EphA5 (NM_004439), EphA6 (ENSP00000374323), EphA7 (NP_004431), EphA8 (NP_065387), EphA10 (NP_001092909), EphB1 (NP_004432), EphB2 (NP_004433), EphB3 (NP_004434), EphB4 (NP_004435) and EphB6 (NP_004436).


Note .
  Figure 6: Sites of somatic mutations in EphA3 identified in lung adenocarcinoma colorectal carcinoma, glioblastoma multiforme, metastatic melanoma and pancreatic cancers (PDAC and AVC).
Germinal To date no germinal mutations in EPHA3 have been associated with disease.
Somatic Somatic mutations in EPHA3 have been frequently detected, including in lung adenocarcinoma (T166N, G187R, S229Y, W250R, M269I, N379K, T393K, A435S, D446Y, S449F, G518L, T660K, D678E, R728L, K761N, G766E, T933M), colorectal carcinoma (T37K, N85S, I621L, S792P, D806N), glioblastoma multiforme (K500N, A971P) metastatic melanoma (G228R) and pancreatic cancer (K207N). Two mutations are reported in haematological malignancies: R897M in mantle cell lymphoma and a truncating E461X mutation in a t(4;14) myeloma (with FGFR3/ WHSC1 (MMSET) translocation). According to the COSMIC catalogue of somatic mutations in cancer ( there are over 300 reported mutations, which are distributed over all regions encoding functional domains, most prominently in the extracellular domains involved in ligand-receptor and receptor-receptor interactions, and in the intracellular kinase domain. Several mutations have been confirmed to inhibit receptor activity and cell surface expression..

Implicated in

Entity Prostate cancer
Note EPHA3 was among the genes whose expression was upregulated during androgen-independent progression in an LNCaP in vitro cell model of prostate cancer. Subsequently, EphA3 was found to correlate with proliferation and survival of prostate cancer cells and tumour growth in mice, and was upregulated in stromal cells at sites of bone metastasis.
Entity Melanoma
Note A melanoma patient with an especially favourable evolution of disease, associated with a very strong and sustained anti-tumour cytotoxic T lymphocyte response, was found to have a lytic CD4 clone that recognised an EphA3 antigen presented by the HLA class II molecule HLA- DRB1*1101. 94% (75 of 80) of melanomas examined expressed EphA3 in contrast to normal melanocytes which do not express detectable EphA3.
Entity Lung cancer, Sarcoma, and Renal cell carcinoma
Note 44% (11 of 25) of small cell lung cancer, 24% (10 of 41) of non-small cell lung cancer, 58% (17 of 29) of sarcomas, and 31% (12 of 38) of renal cell carcinomas expressed EphA3 at levels significantly higher than the corresponding normal tissues.
Entity Liver, gastric, and colorectal cancer
Note High EphA3 expression associated with high invasive capacity and poor overall survival in hepatocellular carcinoma , and with angiogenesis and poor prognosis in gastric cancer. In colorectal cancer, high expression correlates with stem cell marker expression, and with tumour size and grade, infiltration and metastasis.
Entity Hematological tumours
Note Increased expression in 50% of patients with myelodysplastic syndrome, acute myeloid leukaemia or chronic myeloid leukaemia (CML), most prominent on a leukaemia stem cell immunophenotype. Overexpression in a high proportion of the other chronic myeloproliferative diseases was also observed.
Entity Glioma
Note 40% glioma specimens over-expressed EphA3, particularly in mesenchymal subtype. Expression on cancer initiating/stem cell type. Radio-labelled antibody targeting in mouse model inhibited growth.
Entity Other solid tumours: bladder, brain, breast, colon, kidney, liver, lung, melanoma, prostate
Note Over-expressed in high proportion of tumour vasculature and stromal tissues, even when not in the tumour bulk. Expressed on mesenchymal stromal cells recruited from bone marrow. Targeting with activating antibody inhibited tumour growth in mouse models.


Note No reported breakpoints identified to date nor recognised fusion proteins involving EphA3.

To be noted

Soluble forms of EphA3 appear to inhibit tumour angiogenesis and tumour progression suggesting that specific inhibition by soluble EphA3 may be therapeutically useful.
The IIIA4 monoclonal antibody originally raised against LK63 human acute pre-B leukemia cells and used to affinity isolate EphA3 binds the native EphA3 globular ephrin-binding domain with sub-nanomolar affinity (KD ~5x10-10 mol/L). Like ephrin-A5, pre-clustered IIIA4 effectively triggers EphA3 activation, contraction of the cytoskeleton, and cell rounding. Moreover, radio-metal conjugates of ephrin-A5 and IIIA4 retain their EphA3-binding affinity, and in mouse xenografts localise to, and are internalised rapidly into EphA3-positive, human tumours. Treatment of tumour xenografts with IIIA4 alone, or with radio-labelled IIIA4, can inhibit tumour growth. A humanised version of IIIA4 has been developed, with enhanced affinity and antibody-dependent cell-mediated cytotoxicity (ADCC) activity against EphA3-expressing leukemic cells, and is being investigated in Phase I/II clinical trials.

External links

HGNC (Hugo)EPHA3   3387
Entrez_Gene (NCBI)EPHA3  2042  EPH receptor A3
GeneCards (Weizmann)EPHA3
Ensembl hg19 (Hinxton)ENSG00000044524 [Gene_View]  chr3:89156674-89531284 [Contig_View]  EPHA3 [Vega]
Ensembl hg38 (Hinxton)ENSG00000044524 [Gene_View]  chr3:89156674-89531284 [Contig_View]  EPHA3 [Vega]
ICGC DataPortalENSG00000044524
TCGA cBioPortalEPHA3
Genatlas (Paris)EPHA3
SOURCE (Princeton)EPHA3
Genomic and cartography
GoldenPath hg19 (UCSC)EPHA3  -     chr3:89156674-89531284 +  3p11.2   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)EPHA3  -     3p11.2   [Description]    (hg38-Dec_2013)
EnsemblEPHA3 - 3p11.2 [CytoView hg19]  EPHA3 - 3p11.2 [CytoView hg38]
Mapping of homologs : NCBIEPHA3 [Mapview hg19]  EPHA3 [Mapview hg38]
Gene and transcription
Genbank (Entrez)AF213459 AF213460 AK024352 AK291411 BC026247
RefSeq transcript (Entrez)NM_005233 NM_182644
RefSeq genomic (Entrez)NC_000003 NC_018914 NG_023239 NT_022517 NW_004929310
Consensus coding sequences : CCDS (NCBI)EPHA3
Cluster EST : UnigeneHs.123642 [ NCBI ]
CGAP (NCI)Hs.123642
Alternative Splicing : Fast-db (Paris)GSHG0020961
Alternative Splicing GalleryENSG00000044524
Gene ExpressionEPHA3 [ NCBI-GEO ]     EPHA3 [ SEEK ]   EPHA3 [ MEM ]
SOURCE (Princeton)Expression in : [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP29320 (Uniprot)
NextProtP29320  [Medical]  [Publications]
With graphics : InterProP29320
Splice isoforms : SwissVarP29320 (Swissvar)
Catalytic activity : Enzyme2.7.10.1 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   
Domaine pattern : Prosite (Expaxy)EGF_2 (PS01186)    EPH_LBD (PS51550)    FN3 (PS50853)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)    RECEPTOR_TYR_KIN_V_1 (PS00790)    RECEPTOR_TYR_KIN_V_2 (PS00791)    SAM_DOMAIN (PS50105)   
Domains : Interpro (EBI)Eph_TM    Ephrin_rcpt_lig-bd_dom    FN3_dom    Galactose-bd-like    Growth_fac_rcpt_N_dom    Ig-like_fold    Kinase-like_dom    Prot_kinase_dom    Protein_kinase_ATP_BS    SAM    SAM/pointed    SAM_2    Ser-Thr/Tyr_kinase_cat_dom    Tyr-kin_ephrin_A/B_rcpt-like    Tyr_kinase_AS    Tyr_kinase_cat_dom    Tyr_kinase_ephrin_rcpt    Tyr_kinase_rcpt_V_CS   
Related proteins : CluSTrP29320
Domain families : Pfam (Sanger)EphA2_TM (PF14575)    Ephrin_lbd (PF01404)    fn3 (PF00041)    GCC2_GCC3 (PF07699)    Pkinase_Tyr (PF07714)    SAM_2 (PF07647)   
Domain families : Pfam (NCBI)pfam14575    pfam01404    pfam00041    pfam07699    pfam07714    pfam07647   
Domain families : Smart (EMBL)EPH_lbd (SM00615)  FN3 (SM00060)  SAM (SM00454)  TyrKc (SM00219)  
DMDM Disease mutations2042
Blocks (Seattle)P29320
PDB (SRS)2GSF    2QO2    2QO7    2QO9    2QOB    2QOC    2QOD    2QOF    2QOI    2QOK    2QOL    2QON    2QOO    2QOQ    3DZQ    3FXX    3FY2    4G2F    4GK2    4GK3    4GK4    4L0P    4P4C    4P5Q    4P5Z   
PDB (PDBSum)2GSF    2QO2    2QO7    2QO9    2QOB    2QOC    2QOD    2QOF    2QOI    2QOK    2QOL    2QON    2QOO    2QOQ    3DZQ    3FXX    3FY2    4G2F    4GK2    4GK3    4GK4    4L0P    4P4C    4P5Q    4P5Z   
PDB (IMB)2GSF    2QO2    2QO7    2QO9    2QOB    2QOC    2QOD    2QOF    2QOI    2QOK    2QOL    2QON    2QOO    2QOQ    3DZQ    3FXX    3FY2    4G2F    4GK2    4GK3    4GK4    4L0P    4P4C    4P5Q    4P5Z   
PDB (RSDB)2GSF    2QO2    2QO7    2QO9    2QOB    2QOC    2QOD    2QOF    2QOI    2QOK    2QOL    2QON    2QOO    2QOQ    3DZQ    3FXX    3FY2    4G2F    4GK2    4GK3    4GK4    4L0P    4P4C    4P5Q    4P5Z   
Human Protein AtlasENSG00000044524
Peptide AtlasP29320
IPIIPI00298105   IPI00219172   IPI00418427   
Protein Interaction databases
IntAct (EBI)P29320
Ontologies - Pathways
Ontology : AmiGOGPI-linked ephrin receptor activity  protein binding  ATP binding  extracellular region  early endosome  plasma membrane  integral component of plasma membrane  cell adhesion  axon guidance  regulation of epithelial to mesenchymal transition  positive regulation of neuron projection development  cell migration  peptidyl-tyrosine phosphorylation  regulation of actin cytoskeleton organization  regulation of GTPase activity  ephrin receptor signaling pathway  ephrin receptor signaling pathway  regulation of focal adhesion assembly  regulation of microtubule cytoskeleton organization  cellular response to retinoic acid  fasciculation of sensory neuron axon  fasciculation of motor neuron axon  
Ontology : EGO-EBIGPI-linked ephrin receptor activity  protein binding  ATP binding  extracellular region  early endosome  plasma membrane  integral component of plasma membrane  cell adhesion  axon guidance  regulation of epithelial to mesenchymal transition  positive regulation of neuron projection development  cell migration  peptidyl-tyrosine phosphorylation  regulation of actin cytoskeleton organization  regulation of GTPase activity  ephrin receptor signaling pathway  ephrin receptor signaling pathway  regulation of focal adhesion assembly  regulation of microtubule cytoskeleton organization  cellular response to retinoic acid  fasciculation of sensory neuron axon  fasciculation of motor neuron axon  
Pathways : KEGGAxon guidance   
Protein Interaction DatabaseEPHA3
Atlas of Cancer Signalling NetworkEPHA3
Wikipedia pathwaysEPHA3
Gene fusions - Rearrangements
Fusion : MitelmanLCLAT1/EPHA3 [2p23.1/3p11.1]  [t(2;3)(p23;p11)]  
Fusion: TCGALCLAT1 2p23.1 EPHA3 3p11.1 SKCM
Polymorphisms : SNP, variants
NCBI Variation ViewerEPHA3 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EPHA3
Exome Variant ServerEPHA3
Genetic variants : HAPMAPEPHA3
Genomic Variants (DGV)EPHA3 [DGVbeta]
ICGC Data PortalEPHA3 
TCGA Data PortalEPHA3 
Tumor PortalEPHA3
Somatic Mutations in Cancer : COSMICEPHA3 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
DoCM (Curated mutations) EPHA3
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
DECIPHER (Syndromes)3:89156674-89531284
CONAN: Copy Number AnalysisEPHA3 
Mutations and Diseases : HGMDEPHA3
NextProtP29320 [Medical]
Disease Genetic AssociationEPHA3
Huge Navigator EPHA3 [HugePedia]  EPHA3 [HugeCancerGEM]
snp3D : Map Gene to Disease2042
DGIdb (Drug Gene Interaction db)EPHA3
BioCentury BCIQEPHA3
General knowledge
Homologs : HomoloGeneEPHA3
Homology/Alignments : Family Browser (UCSC)EPHA3
Phylogenetic Trees/Animal Genes : TreeFamEPHA3
Chemical/Protein Interactions : CTD2042
Chemical/Pharm GKB GenePA27819
Clinical trialEPHA3
Cancer Resource (Charite)ENSG00000044524
Other databases
PubMed58 Pubmed reference(s) in Entrez


A novel putative tyrosine kinase receptor encoded by the eph gene.
Hirai H, Maru Y, Hagiwara K, Nishida J, Takaku F.
Science. 1987 Dec 18;238(4834):1717-20.
PMID 2825356
Isolation and characterization of a novel receptor-type protein tyrosine kinase (hek) from a human pre-B cell line.
Boyd AW, Ward LD, Wicks IP, Simpson RJ, Salvaris E, Wilks A, Welch K, Loudovaris M, Rockman S, Busmanis I.
J Biol Chem. 1992 Feb 15;267(5):3262-7.
PMID 1737782
Molecular cloning of HEK, the gene encoding a receptor tyrosine kinase expressed by human lymphoid tumor cell lines.
Wicks IP, Wilkinson D, Salvaris E, Boyd AW.
Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1611-5.
PMID 1311845
Expression of the Tyro4/Mek4/Cek4 gene specifically marks a subset of embryonic motor neurons and their muscle targets.
Kilpatrick TJ, Brown A, Lai C, Gassmann M, Goulding M, Lemke G.
Mol Cell Neurosci. 1996 Jan;7(1):62-74.
PMID 8812059
Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor.
Lackmann M, Mann RJ, Kravets L, Smith FM, Bucci TA, Maxwell KF, Howlett GJ, Olsson JE, Vanden Bos T, Cerretti DP, Boyd AW.
J Biol Chem. 1997 Jun 27;272(26):16521-30.
PMID 9195962
PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor.
Hock B, Bohme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rubsamen-Waigmann H, Strebhardt K.
Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9779-84.
PMID 9707552
Distinct subdomains of the EphA3 receptor mediate ligand binding and receptor dimerization.
Lackmann M, Oates AC, Dottori M, Smith FM, Do C, Power M, Kravets L, Boyd AW.
J Biol Chem. 1998 Aug 7;273(32):20228-37.
PMID 9685371
Cloning and characterization of EphA3 (Hek) gene promoter: DNA methylation regulates expression in hematopoietic tumor cells.
Dottori M, Down M, Huttmann A, Fitzpatrick DR, Boyd AW.
Blood. 1999 Oct 1;94(7):2477-86.
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Written04-2009Brett Stringer, Bryan Day, Jennifer McCarron, Martin Lackmann, Andrew Boyd
Leukaemia Foundation Research Laboratory, Queensland Institute of Medical Research, 300 Herston Road, Brisbane Queensland 4006, Australia (BS, BD, JM, AB); Department of Biochemistry and Molecular Biology, PO Box 13D, Monash University, Clayton Victoria 3800, Australia (ML); Department of Medicine, University of Queensland, St Lucia Queensland 4067, Australia (AB)
Updated07-2015Peter W. Janes
Department of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, VIC, 3800, Australia.


This paper should be referenced as such :
Janes Peter W
EPHA3 (EPH receptor A3);
Atlas Genet Cytogenet Oncol Haematol. in press
On line version :
History of this paper:
Stringer, B ; Day, B ; McCarron, J ; Lackmann, M ; Boyd, A. EPHA3 (EPH receptor A3). Atlas Genet Cytogenet Oncol Haematol. 2010;14(3):279-285.

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