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Reviewed, UniProtKB/Swiss-Prot P29317 (EPHA2_HUMAN)

Last modified February 9, 2010. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ephrin type-A receptor 2
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor ECK
    Epithelial cell kinase
Gene names
Name: EPHA2
Synonyms: ECK
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length976 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A3, -A4 and -A5. Plays an important role in angiogenesis and tumor neovascularization. The recruitement of VAV2, VAV3 and PI3-kinase p85 subunit by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly By similarity. Induces apoptosis in a TP53/p53-independent, caspase-8-dependent manner. Ref.10

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Monomer at low protein concentrations (around 10 µM) and forms homodimers at higher concentrations. Forms heterodimers with EFNA1. Interacts with SLA. The phosphorylated form interacts with VAV2, VAV3 and PI3-kinase p85 subunit By similarity. Interacts with INPPL1/SHIP2. Ref.8 Ref.19

Subcellular location

Membrane; Single-pass type I membrane protein Ref.11.

Tissue specificity

Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g., skin, intestine, lung, and ovary. Ref.7

Induction

By ultraviolet radiation (UV) via a TP53/p53-independent, but MAPK-dependent, mechanism. Ref.10

Post-translational modification

Activated by EFNA1 via tyrosine phosphorylation. Phosphorylated residues Tyr-588 and Tyr-594 are required for binding VAV2 and VAV3 while phosphorylated residues Tyr-735 and Tyr-930 are required for binding PI3-kinase p85 subunit. 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 endothelial cell migration. They also play a critical role in transducing EPHA2 signaling in vascular endothelial cells during tumor angiogenesis By similarity. Ref.11 Ref.5 Ref.6 Ref.9 Ref.12 Ref.13 Ref.15

Involvement in disease

Genetic variations in EPHA2 are the cause of susceptibility to cataract cortical age-related type 2 (ARCC2) [MIM:613020]. A developmental punctate opacity common in the cortex and present in most lenses. The cataract is white or cerulean, increases in number with age, but rarely affects vision.

Defects in EPHA2 are the cause of cataract posterior polar type 1 (CTPP1) [MIM:116600]. A subcapsular opacity, usually disk-shaped, located at the back of the lens. It can have a marked effect on visual acuity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 976952Ephrin type-A receptor 2
PRO_0000016800

Regions

Topological domain25 – 534510Extracellular Potential
Transmembrane535 – 55824 Potential
Topological domain559 – 976418Cytoplasmic Potential
Domain328 – 429102Fibronectin type-III 1
Domain435 – 52692Fibronectin type-III 2
Domain613 – 875263Protein kinase
Domain904 – 96865SAM
Nucleotide binding619 – 6279ATP By similarity
Motif974 – 9763PDZ-binding Potential
Compositional bias188 – 325138Cys-rich

Sites

Active site7391Proton acceptor By similarity
Binding site6461ATP By similarity

Amino acid modifications

Modified residue1531Phosphoserine
Modified residue3731Phosphoserine
Modified residue5701Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue5751Phosphotyrosine Ref.6 Ref.12 Ref.15
Modified residue5791Phosphoserine Ref.12
Modified residue5871Phosphothreonine
Modified residue5881Phosphotyrosine; by autocatalysis By similarity
Modified residue5931Phosphothreonine
Modified residue5941Phosphotyrosine; by autocatalysis Ref.5 Ref.6 Ref.9 Ref.12 Ref.15
Modified residue6281Phosphotyrosine Ref.12
Modified residue6471Phosphothreonine Ref.12
Modified residue7351Phosphotyrosine; by autocatalysis By similarity
Modified residue7711Phosphothreonine
Modified residue7721Phosphotyrosine; by autocatalysis Ref.5 Ref.6 Ref.9 Ref.12 Ref.15
Modified residue7901Phosphoserine
Modified residue7911Phosphotyrosine
Modified residue8691Phosphoserine
Modified residue8801Phosphoserine
Modified residue8921Phosphoserine Ref.13
Modified residue8971Phosphoserine Ref.9 Ref.12
Modified residue8981Phosphothreonine Ref.9 Ref.12
Modified residue8991Phosphoserine Ref.12
Modified residue9011Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue9101Phosphoserine
Modified residue9211Phosphotyrosine; by autocatalysis Potential
Modified residue9301Phosphotyrosine Ref.5
Modified residue9601Phosphotyrosine Ref.15
Glycosylation4071N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Ref.14
Disulfide bond70 ↔ 188 Ref.19
Disulfide bond105 ↔ 115 Ref.19

Natural variations

Natural variant991K → N: dbSNP rs1058372.
VAR_055989
Natural variant3911G → R: dbSNP rs34192549. Ref.22
VAR_042121
Natural variant5111T → M: dbSNP rs55747232. Ref.22
VAR_042122
Natural variant5681R → H: dbSNP rs56198600. Ref.22
VAR_042123
Natural variant6311M → T: dbSNP rs34021505.
VAR_055990
Natural variant7211R → Q in ARCC2; alters EPHA2 signaling.
VAR_062532
Natural variant7771G → S in a gastric adenocarcinoma sample; somatic mutation. Ref.22
VAR_042124
Natural variant8761R → H: dbSNP rs35903225. Ref.22
VAR_042125
Natural variant9401T → I in CTPP1.
VAR_058907
Natural variant9481G → W in CTPP1.
VAR_058908

Experimental info

Mutagenesis1031R → E: Significantly reduced response to EFNA1. Ref.19
Sequence conflict94 – 996IFIELK → NNFELN in AAA53375. Ref.1

Secondary structure

..................................................... 976
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29317-1 [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: 845D7E1BBCCAACCC

FASTA976108,266
        10         20         30         40         50         60 
MELQAARACF ALLWGCALAA AAAAQGKEVV LLDFAAAGGE LGWLTHPYGK GWDLMQNIMN 

        70         80         90        100        110        120 
DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF TVRDCNSFPG GASSCKETFN 

       130        140        150        160        170        180 
LYYAESDLDY GTNFQKRLFT KIDTIAPDEI TVSSDFEARH VKLNVEERSV GPLTRKGFYL 

       190        200        210        220        230        240 
AFQDIGACVA LLSVRVYYKK CPELLQGLAH FPETIAGSDA PSLATVAGTC VDHAVVPPGG 

       250        260        270        280        290        300 
EEPRMHCAVD GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEASESPC LECPEHTLPS 

       310        320        330        340        350        360 
PEGATSCECE EGFFRAPQDP ASMPCTRPPS APHYLTAVGM GAKVELRWTP PQDSGGREDI 

       370        380        390        400        410        420 
VYSVTCEQCW PESGECGPCE ASVRYSEPPH GLTRTSVTVS DLEPHMNYTF TVEARNGVSG 

       430        440        450        460        470        480 
LVTSRSFRTA SVSINQTEPP KVRLEGRSTT SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN 

       490        500        510        520        530        540 
SYNVRRTEGF SVTLDDLAPD TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGNLAVIGG 

       550        560        570        580        590        600 
VAVGVVLLLV LAGVGFFIHR RRKNQRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA 

       610        620        630        640        650        660 
VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG MLKTSSGKKE VPVAIKTLKA GYTEKQRVDF 

       670        680        690        700        710        720 
LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEYMENGAL DKFLREKDGE FSVLQLVGML 

       730        740        750        760        770        780 
RGIAAGMKYL ANMNYVHRDL AARNILVNSN LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP 

       790        800        810        820        830        840 
IRWTAPEAIS YRKFTSASDV WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM 

       850        860        870        880        890        900 
DCPSAIYQLM MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG 

       910        920        930        940        950        960 
SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR LPGHQKRIAY 

       970 
SLLGLKDQVN TVGIPI 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases."
Lindberg R.A., Hunter T.
Mol. Cell. Biol. 10:6316-6324(1990) [PubMed: 2174105] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Epithelium.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[5]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-588; TYR-594; TYR-772; TYR-921 AND TYR-930, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-575; TYR-588; TYR-594 AND TYR-772, MASS SPECTROMETRY.
[7]"Ephrin-A1 is a negative regulator in glioma through down-regulation of EphA2 and FAK."
Liu D.-P., Wang Y., Koeffler H.P., Xie D.
Int. J. Oncol. 30:865-871(2007) [PubMed: 17332925] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation."
Zhuang G., Hunter S., Hwang Y., Chen J.
J. Biol. Chem. 282:2683-2694(2007) [PubMed: 17135240] [Abstract]
Cited for: INTERACTION WITH INPPL1.
[9]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; TYR-594; TYR-772; SER-897; THR-898 AND SER-901, MASS SPECTROMETRY.
[10]"EphA2 is an essential mediator of UV radiation-induced apoptosis."
Zhang G., Njauw C.-N., Park J.M., Naruse C., Asano M., Tsao H.
Cancer Res. 68:1691-1696(2008) [PubMed: 18339848] [Abstract]
Cited for: FUNCTION, INDUCTION.
[11]"Soluble monomeric EphrinA1 is released from tumor cells and is a functional ligand for the EphA2 receptor."
Wykosky J., Palma E., Gibo D.M., Ringler S., Turner C.P., Debinski W.
Oncogene 27:7260-7273(2008) [PubMed: 18794797] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; TYR-575; SER-579; TYR-594; TYR-628; THR-647; TYR-772; SER-897; THR-898; SER-899 AND SER-901, MASS SPECTROMETRY.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-892 AND SER-901, MASS SPECTROMETRY.
[14]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-435, MASS SPECTROMETRY.
Tissue: Liver.
[15]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-575; TYR-588; TYR-594; TYR-772 AND TYR-960, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[16]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-373; SER-570; TYR-575; THR-587; TYR-588; THR-593; TYR-594; TYR-628; THR-647; THR-771; TYR-772; SER-790; TYR-791; SER-869; SER-880; SER-897; THR-898; SER-899; SER-901; SER-910 AND TYR-960, MASS SPECTROMETRY.
[17]"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography."
Nowakowski J., Cronin C.N., McRee D.E., Knuth M.W., Nelson C.G., Pavletich N.P., Rogers J., Sang B.C., Scheibe D.N., Swanson R.V., Thompson D.A.
Structure 10:1659-1667(2002) [PubMed: 12467573] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 596-900.
[18]"Solution structure of the C-terminal SAM-domain of EPHAA2: ephrin type-A receptor 2 precursor (EC 2.7.10.1)."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 902-976.
[19]"Ligand recognition by A-class Eph receptors: crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex."
Himanen J.P., Goldgur Y., Miao H., Myshkin E., Guo H., Buck M., Nguyen M., Rajashankar K.R., Wang B., Nikolov D.B.
EMBO Rep. 10:722-728(2009) [PubMed: 19525919] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 28-201, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-201 IN COMPLEX WITH EFNA1, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ARG-103.
[20]"Ephrin A1 bound to the ligand binding domain of the human ephrin A2 (epha2) receptor protein kinase."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-202, DISULFIDE BOND.
[21]"Left-handed dimer of EPHA2 transmembrane domain helix packing diversity among receptor tyrosine kinases."
Mayzel M.L., Bocharov E.V., Volynsky P.E., Arseniev A.S.
Submitted (AUG-2009) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 523-563.
[22]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-391; MET-511; HIS-568; SER-777 AND HIS-876.
[23]"The EPHA2 gene is associated with cataracts linked to chromosome 1p."
Shiels A., Bennett T.M., Knopf H.L.S., Maraini G., Li A., Jiao X., Hejtmancik J.F.
Mol. Vis. 14:2042-2055(2008) [PubMed: 19005574] [Abstract]
Cited for: VARIANT CTPP1 TRP-948, INVOLVEMENT IN AGE-RELATED CATARACTS.
[24]"Mutations of the EPHA2 receptor tyrosine kinase gene cause autosomal dominant congenital cataract."
Zhang T., Hua R., Xiao W., Burdon K.P., Bhattacharya S.S., Craig J.E., Shang D., Zhao X., Mackey D.A., Moore A.T., Luo Y., Zhang J., Zhang X.
Hum. Mutat. 30:E603-E611(2009) [PubMed: 19306328] [Abstract]
Cited for: VARIANT CTPP1 ILE-940.
[25]"EPHA2 is associated with age-related cortical cataract in mice and humans."
Jun G., Guo H., Klein B.E., Klein R., Wang J.J., Mitchell P., Miao H., Lee K.E., Joshi T., Buck M., Chugha P., Bardenstein D., Klein A.P., Bailey-Wilson J.E., Gong X., Spector T.D., Andrew T., Hammond C.J. expand/collapse author list , Elston R.C., Iyengar S.K., Wang B.
PLoS Genet. 5:E1000584-E1000584(2009) [PubMed: 19649315] [Abstract]
Cited for: VARIANT ARCC2 GLN-721, CHARACTERIZATION OF VARIANT ARCC2 GLN-721.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59371 mRNA. Translation: AAA53375.1.
AL451042 Genomic DNA. Translation: CAH71943.1.
CH471167 Genomic DNA. Translation: EAW51769.1.
BC037166 mRNA. Translation: AAH37166.1.
IPIIPI00021267.
PIRA36355.
RefSeqNP_004422.2.
UniGeneHs.171596

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MQBX-ray2.30A/B596-900[»]
2E8NNMR-A902-976[»]
2K9YNMR-A/B523-563[»]
3C8XX-ray1.95A23-202[»]
3CZUX-ray2.65A23-202[»]
3FL7X-ray2.50A23-531[»]
3HEIX-ray2.00A/C/E/G/I/K/M/O28-201[»]
3HPNX-ray2.52A/B/C/D/E/F28-201[»]
3KKAX-ray2.40C/D/E903-971[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-96N.
STRINGP29317.

PTM databases

PhosphoSiteP29317.

Proteomic databases

PRIDEP29317.

Genome annotation databases

EnsemblENST00000358432; ENSP00000351209; ENSG00000142627; Homo sapiens. [Genome view]
ENST00000407976; ENSP00000384858; ENSG00000142627; Homo sapiens. [Genome view]
GeneID1969.
KEGGhsa:1969.

Organism-specific databases

CTD1969.
GeneCardsGC01M016323.
HGNCHGNC:3386. EPHA2.
HPACAB010464.
MIM116600. phenotype.
176946. gene.
613020. phenotype.
Orphanet98993. Cataract, posterior polar.
PharmGKBPA27818.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08660.
HOGENOMHBG755340.
HOVERGENP29317.
InParanoidP29317.
OMAVHEFQTL.
OrthoDBEOG9JDKSD.
PhylomeDBP29317.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBepha_fwdpathway. EPHA forward signaling.
epha2_fwdpathway. EPHA2 forward signaling.
ephrina_ephapathway. EphrinA-EPHA pathway.

Gene expression databases

ArrayExpressP29317.
BgeeP29317.
CleanExHS_EPHA2.
GenevestigatorP29317.
GermOnlineENSG00000142627. Homo sapiens.

Family and domain databases

InterProIPR001090. Ephrin_rcpt_lig-bd.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR010993. SAM_homology.
IPR013761. SAM_type.
IPR021129. SAM_type1.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
IPR016257. Tyr_prot_kinase_ephrin_rcpt.
IPR001426. Tyr_prot_kinase_rcpt_V_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
G3DSA:1.10.150.50. SAM_type. 1 hit.
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01254. Dasatinib.
NextBio7983.
SOURCESearch...

Entry information

Entry nameEPHA2_HUMAN
AccessionPrimary (citable) accession number: P29317
Secondary accession number(s): Q8N3Z2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 5, 2009
Last modified: February 9, 2010
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents