Atlas of Genetics and Cytogenetics in Oncology and Haematology

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EPHA1 (EPH receptor A1)

Written2008-12Brett Stringer, Nirmitha Herath, Shannon Duffy, Mark Coulthard, Andrew Boyd
Leukaemia Foundation Research Laboratory, Queensland Institute of Medical Research, 300 Herston Road, Brisbane Qld 4006, Australia (BS, NH, SD, MC, AB); Royal Children's Hospital, Herston Qld 4006, Australia (MC); University of Queensland, St Lucia Qld 4067, Australia (AB)

(Note : for Links provided by Atlas : click)


Alias_symbol (synonym)EPH
Other alias
LocusID (NCBI) 2041
Atlas_Id 40461
Location 7q34  [Link to chromosome band 7q34]
Location_base_pair Starts at 143391112 and ends at 143408892 bp from pter ( according to hg19-Feb_2009)  [Mapping EPHA1.png]
Local_order (cen) ZYX ->, 8bp, <- EPHA1, 34.5kb, TASR60 -> (tel)
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
EPHA1 (7q34) / EPHA1 (7q34)LMBR1 (7q36.3) / EPHA1 (7q34)USP32 (17q23.1) / EPHA1 (7q34)


  Genomic neighbourhood and organisation of EPHA1.
Description EPHA1 consists of 18 exons and 17 introns and spans 17.78kb of genomic DNA. EPHA1 is located within the human tilepath clone RP11-811J9.
Transcription 3,359 nucleotide mRNA. Two alternative splice variants, predicted to result in truncation within the extracellular domain of EphA1, have been reported.
Pseudogene None identified.


Note EphA1 was isolated originally from an erythropoietin producing hepatoma cell line, from which its name, and the name of its gene family, derives.
  Domain organisation of EphA1.
Description The EPHA1 gene encodes a 976 amino acid protein with a calculated molecular weight of 108,126.89 and an isoelectric point of 6.6254. Amino acids 1-25 constitute a signal peptide.
EphA1 is the founding member of what is recognised as the largest subfamily of the receptor tyrosine kinases. This is an evolutionarily ancient protein group 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. 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. Eph-ephrin binding involves cell-cell contact. Upon binding, both Eph and ephrin proteins on respective cells dimerise, and undergo higher order clustering. This results in signalling within both the Eph- and ephrin-bearing cells (bidirectional signalling) and either subsequent adhesion or repulsion of the interacting cells. Cell-cell contact, and thus Eph-ephrin signalling, may be terminated either by enzymatic cleavage of the extracellular domain of the Eph receptor or ephrin ligand or endocytosis of Eph-ephrin complexes.
The high affinity ligands for EphA1 are ephrin-A1 and ephrin-A3. EphA1 also binds fibronectin, a non-activating ligand.
Expression Embryonic stem (ES) cells and embryoid bodies differentiated from ES cells in vitro; dynamic and regionalised expression during murine embryogenesis (including epiblast, primitive streak, paraxial mesoderm, tail bud mesoderm, distal limb bud); human lung, small intestinal, kidney, bladder, thymus, skin and colon. Murine adult epithelial tissues (including epidermis of skin and vagina, endometrium, renal collecting system). Rat normal liver, kidney, lung. Human tumours and cell lines of epithelial origin.
Localisation Membrane; single-pass type I membrane protein.
Function Not yet entirely established. Generally repulsive interaction with its high affinity ligands ephrin-A1 and ephrin-A3. Transgenic expression of EphA1 in the blastula of pre-implantation mice is lethal (Duffy et al., unpublished). EphA1 homozygous null mice exhibit kinked tails (80%) and imperforate vagina (18% of females). The apparent absence of EphA1 in fish (zebrafish, medaka, fugu) and amphibia (Xenopus) and its emergence in vertebrates with reptiles (anole lizard) and birds (chicken) hints at an association with the transition of life from an aquatic to terrestrial environment. The presence of a membrane-embedded ionogenic Glu547 residue within the transmembrane domain of EphA1 also is unique among the Eph receptors. The structural-dynamic properties of the transmembrane domain have been shown to be dependent on the ionisation state of this residue, a finding that implies that the conformational flexibility and activation of the EphA1 receptor can be regulated by such external and local factors as pH and lipid composition of the membrane, a finding which may be of particular relevance to EphA1 function in the skin and kidney.
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).


Germinal No germinal mutations identified to be associated with cancer so far.
Somatic Rare. A single heterozygous missense mutation E703K within the tyrosine kinase domain has been reported for a lobular breast carcinoma.

Implicated in

Entity Colorectal cancer
Note An immunohistochemical study of 20 colorectal adenomas and 111 colorectal carcinomas specimens detected EphA1 protein expression in all adenomas and reduced expression in 54% of colorectal cancers. Reduced expression of EphA1 was found more often in male patients (P=0.028) and in patients with poor differentiation (P=0.027), greater depth of wall invasion (P=0.003), lymph node metastasis (P=0.034), and advanced tumour stage (P=0.003).
Prognosis Patients with colorectal cancer in this study with reduced EphA1 expression had a poor overall survival (P=0.059). Reduced EphA1 expression in patients over 55 years or with rectal cancers and sigmoid colon cancers was associated with a poor overall survival (P=0.034 and 0.015, respectively).
Entity Nonmelanoma skin cancer
Note EphA1, which in human adults is expressed in the epidermis of the skin, is significantly downregulated at the protein level in basal cell and squamous cell carcinomas.
Entity Glioblastoma
Note EphA1 expression is significantly downregulated in human glioblastoma and glioblastoma cell lines.
Entity Breast cancer
Note Down regulation of EphA1 was associated with increased invasiveness in a breast cancer progression model using quantitative real time RT-PCR expression profiles of EphA1 mRNA in MCF-10A, MCF-7, and MDA-MB-231 cells, representing normal breast, non-invasive breast tumour, and invasive tumour, respectively, based on their characteristic phenotypes in Matrigel matrix.
Entity Prostate cancer
Note EphA1 mRNA transcript expression was found to decrease progressively in a panel of human prostate cancer cell lines representative of the transition from normal prostate to primary prostate tumour to metastatic tumour.
Entity Ovarian cancer
Note Overexpression of EphA1 in the presence of elevated expression of its high affinity ligand ephrin-A1 was observed with more aggressive ovarian cancer phenotypes.
Entity Head and neck squamous cell carcinoma (HNSCC )
Note EphA1 was reported to be highly expressed in HNSCC using an approach that cloned receptor tyrosine kinases by RT-PCR using degenerate receptor tyrosine kinase primers from seven HNSCC specimens and confirmed abundant EphA1 protein expression by immunohistochemistry in eight independent HNSCC specimens.


Approximate likelihood-ratio test for branches: A fast, accurate, and powerful alternative.
Anisimova M, Gascuel O.
Syst Biol. 2006 Aug;55(4):539-52.
PMID 16785212
Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1.
Bocharov EV, Mayzel ML, Volynsky PE, Goncharuk MV, Ermolyuk YS, Schulga AA, Artemenko EO, Efremov RG, Arseniev AS.
J Biol Chem. 2008 Oct 24;283(43):29385-95. Epub 2008 Aug 26.
PMID 18728013
Signals from Eph and ephrin proteins: a developmental tool kit.
Boyd AW, Lackmann M.
Sci STKE. 2001 Dec 11;2001(112):RE20.
PMID 11741094
Selection of conserved blocks from multiple alignments for their use in phylogenetic analysis.
Castresana J.
Mol Biol Evol. 2000 Apr;17(4):540-52.
PMID 10742046
TreeDyn: towards dynamic graphics and annotations for analyses of trees.
Chevenet F, Brun C, Banuls AL, Jacq B, Christen R.
BMC Bioinformatics. 2006 Oct 10;7:439.
PMID 17032440
Characterization of the Epha1 receptor tyrosine kinase: expression in epithelial tissues.
Coulthard MG, Lickliter JD, Subanesan N, Chen K, Webb GC, Lowry AJ, Koblar S, Bottema CD, Boyd AW.
Growth Factors. 2001;18(4):303-17.
PMID 11519828 robust phylogenetic analysis for the non-specialist.
Dereeper A, Guignon V, Blanc G, Audic S, Buffet S, Chevenet F, Dufayard JF, Guindon S, Lefort V, Lescot M, Claverie JM, Gascuel O.
Nucleic Acids Res. 2008 Jul 1;36(Web Server issue):W465-9. Epub 2008 Apr 19.
PMID 18424797
Downregulation of EphA1 in colorectal carcinomas correlates with invasion and metastasis.
Dong Y, Wang J, Sheng Z, Li G, Ma H, Wang X, Zhang R, Lu G, Hu Q, Sugimura H, Zhou X.
Mod Pathol. 2009 Jan;22(1):151-60. Epub 2008 Nov 14.
PMID 19011600
Eph family functions from an evolutionary perspective.
Drescher U.
Curr Opin Genet Dev. 2002 Aug;12(4):397-402.
PMID 12100883
Generation and characterization of EphA1 receptor tyrosine kinase reporter knockout mice.
Duffy SL, Coulthard MG, Spanevello MD, Herath NI, Yeadon TM, McCarron JK, Carter JC, Tonks ID, Kay GF, Phillips GE, Boyd AW.
Genesis. 2008 Oct;46(10):553-61.
PMID 18802966
Expression analysis of the Epha1 receptor tyrosine kinase and its high-affinity ligands Efna1 and Efna3 during early mouse development.
Duffy SL, Steiner KA, Tam PP, Boyd AW.
Gene Expr Patterns. 2006 Oct;6(7):719-23. Epub 2006 Feb 8.
PMID 16466970
MUSCLE: multiple sequence alignment with high accuracy and high throughput.
Edgar RC.
Nucleic Acids Res. 2004 Mar 19;32(5):1792-7. Print 2004.
PMID 15034147
Invasiveness of breast carcinoma cells and transcript profile: Eph receptors and ephrin ligands as molecular markers of potential diagnostic and prognostic application.
Fox BP, Kandpal RP.
Biochem Biophys Res Commun. 2004 Jun 11;318(4):882-92.
PMID 15147954
Potential clinical relevance of Eph receptors and ephrin ligands expressed in prostate carcinoma cell lines.
Fox BP, Tabone CJ, Kandpal RP.
Biochem Biophys Res Commun. 2006 Apr 21;342(4):1263-72. Epub 2006 Feb 28.
PMID 16516143
A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood.
Guindon S, Gascuel O.
Syst Biol. 2003 Oct;52(5):696-704.
PMID 14530136
Differential gene expression of Eph receptors and ephrins in benign human tissues and cancers.
Hafner C, Schmitz G, Meyer S, Bataille F, Hau P, Langmann T, Dietmaier W, Landthaler M, Vogt T.
Clin Chem. 2004 Mar;50(3):490-9. Epub 2004 Jan 15.
PMID 14726470
Over-expression of Eph and ephrin genes in advanced ovarian cancer: ephrin gene expression correlates with shortened survival.
Herath NI, Spanevello MD, Sabesan S, Newton T, Cummings M, Duffy S, Lincoln D, Boyle G, Parsons PG, Boyd AW.
BMC Cancer. 2006 Jun 1;6:144.
PMID 16737551
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
Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis.
Jin P, Zhang J, Sumariwalla PF, Ni I, Jorgensen B, Crawford D, Phillips S, Feldmann M, Shepard HM, Paleolog EM.
Arthritis Res Ther. 2008;10(4):R73. Epub 2008 Jul 1.
PMID 18593464
Identification of tyrosine kinases overexpressed in head and neck cancer.
Lin HS, Berry GJ, Fee WE Jr, Terris DJ, Sun Z.
Arch Otolaryngol Head Neck Surg. 2004 Mar;130(3):311-6.
PMID 15023838
Overexpression confers an oncogenic potential upon the eph gene.
Maru Y, Hirai H, Takaku F.
Oncogene. 1990 Mar;5(3):445-7.
PMID 2314900
Fibronectin type I repeat is a nonactivating ligand for EphA1 and inhibits ATF3-dependent angiogenesis.
Masuda J, Usui R, Maru Y.
J Biol Chem. 2008 May 9;283(19):13148-55. Epub 2008 Feb 28.
PMID 18308734
Genomic structure of the EPHA1 receptor tyrosine kinase gene.
Owshalimpur D, Kelley MJ.
Mol Cell Probes. 1999 Jun;13(3):169-73.
PMID 10369740
Eph-ephrin bidirectional signaling in physiology and disease.
Pasquale EB.
Cell. 2008 Apr 4;133(1):38-52.
PMID 18394988
A screen of the complete protein kinase gene family identifies diverse patterns of somatic mutations in human breast cancer.
Stephens P, Edkins S, Davies H, Greenman C, Cox C, Hunter C, Bignell G, Teague J, Smith R, Stevens C, O'Meara S, Parker A, Tarpey P, Avis T, Barthorpe A, Brackenbury L, Buck G, Butler A, Clements J, Cole J, Dicks E, Edwards K, Forbes S, Gorton M, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jones D, Kosmidou V, Laman R, Lugg R, Menzies A, Perry J, Petty R, Raine K, Shepherd R, Small A, Solomon H, Stephens Y, Tofts C, Varian J, Webb A, West S, Widaa S, Yates A, Brasseur F, Cooper CS, Flanagan AM, Green A, Knowles M, Leung SY, Looijenga LH, Malkowicz B, Pierotti MA, Teh B, Yuen ST, Nicholson AG, Lakhani S, Easton DF, Weber BL, Stratton MR, Futreal PA, Wooster R.
Nat Genet. 2005 Jun;37(6):590-2. Epub 2005 May 22.
PMID 15908952


This paper should be referenced as such :
Stringer, B ; Herath, N ; Duffy, S ; Coulthard, M ; Boyd, A
EPHA1 (EPH receptor A1)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(11):817-820.
Free journal version : [ pdf ]   [ DOI ]
On line version :

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 2 ]

Solid Tumors TT_t0707q35q36ID107737 TT_t0717q35q23ID107470

External links

HGNC (Hugo)EPHA1   3385
Entrez_Gene (NCBI)EPHA1  2041  EPH receptor A1
GeneCards (Weizmann)EPHA1
Ensembl hg19 (Hinxton)ENSG00000146904 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000146904 [Gene_View]  ENSG00000146904 [Sequence]  chr7:143391112-143408892 [Contig_View]  EPHA1 [Vega]
ICGC DataPortalENSG00000146904
TCGA cBioPortalEPHA1
Genatlas (Paris)EPHA1
SOURCE (Princeton)EPHA1
Genetics Home Reference (NIH)EPHA1
Genomic and cartography
GoldenPath hg38 (UCSC)EPHA1  -     chr7:143391112-143408892 -  7q34-q35   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)EPHA1  -     7q34-q35   [Description]    (hg19-Feb_2009)
GoldenPathEPHA1 - 7q34-q35 [CytoView hg19]  EPHA1 - 7q34-q35 [CytoView hg38]
Mapping of homologs : NCBIEPHA1 [Mapview hg19]  EPHA1 [Mapview hg38]
Gene and transcription
Genbank (Entrez)AA723562 AA723620 AA788809 AI057542 AK290351
RefSeq transcript (Entrez)NM_005232
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)EPHA1
Alternative Splicing GalleryENSG00000146904
Gene ExpressionEPHA1 [ NCBI-GEO ]   EPHA1 [ EBI - ARRAY_EXPRESS ]   EPHA1 [ SEEK ]   EPHA1 [ MEM ]
Gene Expression Viewer (FireBrowse)EPHA1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2041
GTEX Portal (Tissue expression)EPHA1
Human Protein AtlasENSG00000146904-EPHA1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP21709   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP21709  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP21709
Splice isoforms : SwissVarP21709
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    EphA1_rcpt_lig-bd    Ephrin_rcpt_lig-bd_dom    FN3_dom    FN3_sf    Galactose-bd-like_sf    Growth_fac_rcpt_cys_sf    Ig-like_fold    Kinase-like_dom_sf    Prot_kinase_dom    Protein_kinase_ATP_BS    SAM    SAM/pointed_sf    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   
Domain families : Pfam (Sanger)EphA2_TM (PF14575)    Ephrin_lbd (PF01404)    fn3 (PF00041)    Pkinase_Tyr (PF07714)    SAM_1 (PF00536)   
Domain families : Pfam (NCBI)pfam14575    pfam01404    pfam00041    pfam07714    pfam00536   
Domain families : Smart (EMBL)EPH_lbd (SM00615)  Ephrin_rec_like (SM01411)  FN3 (SM00060)  SAM (SM00454)  TyrKc (SM00219)  
Conserved Domain (NCBI)EPHA1
DMDM Disease mutations2041
Blocks (Seattle)EPHA1
PDB (RSDB)2K1K    2K1L    3HIL    3KKA   
PDB Europe2K1K    2K1L    3HIL    3KKA   
PDB (PDBSum)2K1K    2K1L    3HIL    3KKA   
PDB (IMB)2K1K    2K1L    3HIL    3KKA   
Structural Biology KnowledgeBase2K1K    2K1L    3HIL    3KKA   
SCOP (Structural Classification of Proteins)2K1K    2K1L    3HIL    3KKA   
CATH (Classification of proteins structures)2K1K    2K1L    3HIL    3KKA   
Human Protein Atlas [tissue]ENSG00000146904-EPHA1 [tissue]
Peptide AtlasP21709
IPIIPI00294250   IPI00908698   IPI00911030   
Protein Interaction databases
IntAct (EBI)P21709
Ontologies - Pathways
Ontology : AmiGOangiogenesis  positive regulation of cell-matrix adhesion  protein kinase activity  transmembrane receptor protein tyrosine kinase activity  transmembrane-ephrin receptor activity  transmembrane-ephrin receptor activity  ATP binding  plasma membrane  integral component of plasma membrane  integral component of plasma membrane  negative regulation of protein kinase activity  cell surface receptor signaling pathway  transmembrane receptor protein tyrosine kinase signaling pathway  axon guidance  positive regulation of cell proliferation  peptidyl-tyrosine phosphorylation  protein kinase binding  positive regulation of cell migration  negative regulation of cell migration  substrate adhesion-dependent cell spreading  somatic stem cell population maintenance  neuron projection  regulation of GTPase activity  dendritic spine  receptor complex  positive regulation of angiogenesis  protein autophosphorylation  ephrin receptor signaling pathway  positive regulation of stress fiber assembly  activation of GTPase activity  
Ontology : EGO-EBIangiogenesis  positive regulation of cell-matrix adhesion  protein kinase activity  transmembrane receptor protein tyrosine kinase activity  transmembrane-ephrin receptor activity  transmembrane-ephrin receptor activity  ATP binding  plasma membrane  integral component of plasma membrane  integral component of plasma membrane  negative regulation of protein kinase activity  cell surface receptor signaling pathway  transmembrane receptor protein tyrosine kinase signaling pathway  axon guidance  positive regulation of cell proliferation  peptidyl-tyrosine phosphorylation  protein kinase binding  positive regulation of cell migration  negative regulation of cell migration  substrate adhesion-dependent cell spreading  somatic stem cell population maintenance  neuron projection  regulation of GTPase activity  dendritic spine  receptor complex  positive regulation of angiogenesis  protein autophosphorylation  ephrin receptor signaling pathway  positive regulation of stress fiber assembly  activation of GTPase activity  
Pathways : KEGGAxon guidance   
REACTOMEP21709 [protein]
REACTOME PathwaysR-HSA-3928665 [pathway]   
NDEx NetworkEPHA1
Atlas of Cancer Signalling NetworkEPHA1
Wikipedia pathwaysEPHA1
Orthology - Evolution
GeneTree (enSembl)ENSG00000146904
Phylogenetic Trees/Animal Genes : TreeFamEPHA1
Homologs : HomoloGeneEPHA1
Homology/Alignments : Family Browser (UCSC)EPHA1
Gene fusions - Rearrangements
Fusion : MitelmanLMBR1/EPHA1 [7q36.3/7q34]  [t(7;7)(q35;q36)]  
Fusion : MitelmanUSP32/EPHA1 [17q23.1/7q34]  [t(7;17)(q35;q23)]  
Fusion PortalLMBR1 7q36.3 EPHA1 7q34 BRCA
Fusion PortalUSP32 17q23.1 EPHA1 7q34 LUSC
Fusion : FusionGDB11800    19871    24091    41050   
Fusion : Fusion_HubEPHA1--EPHA1    EPHA1--RGL4    EPHA1--USP32    LMBR1--EPHA1    USP32--EPHA1   
Fusion : QuiverEPHA1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerEPHA1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EPHA1
Exome Variant ServerEPHA1
ExAC (Exome Aggregation Consortium)ENSG00000146904
GNOMAD BrowserENSG00000146904
Varsome BrowserEPHA1
Genetic variants : HAPMAP2041
Genomic Variants (DGV)EPHA1 [DGVbeta]
DECIPHEREPHA1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisEPHA1 
ICGC Data PortalEPHA1 
TCGA Data PortalEPHA1 
Broad Tumor PortalEPHA1
OASIS PortalEPHA1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICEPHA1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DEPHA1
Mutations and Diseases : HGMDEPHA1
intOGen PortalEPHA1
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
BioMutasearch EPHA1
DgiDB (Drug Gene Interaction Database)EPHA1
DoCM (Curated mutations)EPHA1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)EPHA1 (select a term)
NCG5 (London)EPHA1
Cancer3DEPHA1(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry EPHA1
NextProtP21709 [Medical]
Target ValidationEPHA1
Huge Navigator EPHA1 [HugePedia]
snp3D : Map Gene to Disease2041
BioCentury BCIQEPHA1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2041
Chemical/Pharm GKB GenePA27817
Clinical trialEPHA1
canSAR (ICR)EPHA1 (select the gene name)
DataMed IndexEPHA1
PubMed73 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Wed Feb 19 15:37:57 CET 2020

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