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Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK)

 EPHA2_HUMAN             Reviewed;         976 AA.
P29317; B5A968; Q8N3Z2;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
12-SEP-2018, entry version 216.
RecName: Full=Ephrin type-A receptor 2;
EC=2.7.10.1;
AltName: Full=Epithelial cell kinase;
AltName: Full=Tyrosine-protein kinase receptor ECK;
Flags: Precursor;
Name=EPHA2; Synonyms=ECK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND
AUTOPHOSPHORYLATION.
TISSUE=Epithelium;
PubMed=2174105; DOI=10.1128/MCB.10.12.6316;
Lindberg R.A., Hunter T.;
"cDNA cloning and characterization of eck, an epithelial cell receptor
protein-tyrosine kinase in the eph/elk family of protein kinases.";
Mol. Cell. Biol. 10:6316-6324(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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., 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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NOMENCLATURE.
PubMed=9267020;
Eph nomenclature committee;
"Unified nomenclature for Eph family receptors and their ligands, the
ephrins.";
Cell 90:403-404(1997).
[7]
FUNCTION IN INTEGRIN-MEDIATED CELL ADHESION, FUNCTION IN CELL
MIGRATION, PHOSPHORYLATION, INTERACTION WITH PTK2/FAK1 AND PTPN11, AND
SUBCELLULAR LOCATION.
PubMed=10655584; DOI=10.1038/35000008;
Miao H., Burnett E., Kinch M., Simon E., Wang B.;
"Activation of EphA2 kinase suppresses integrin function and causes
focal-adhesion-kinase dephosphorylation.";
Nat. Cell Biol. 2:62-69(2000).
[8]
ONCOGENICITY.
PubMed=11280802;
Zelinski D.P., Zantek N.D., Stewart J.C., Irizarry A.R., Kinch M.S.;
"EphA2 overexpression causes tumorigenesis of mammary epithelial
cells.";
Cancer Res. 61:2301-2306(2001).
[9]
INTERACTION WITH ACP1, AND DEPHOSPHORYLATION BY ACP1.
PubMed=12167657; DOI=10.1074/jbc.M207127200;
Kikawa K.D., Vidale D.R., Van Etten R.L., Kinch M.S.;
"Regulation of the EphA2 kinase by the low molecular weight tyrosine
phosphatase induces transformation.";
J. Biol. Chem. 277:39274-39279(2002).
[10]
FUNCTION IN CELL-CELL INTERACTION, INTERACTION WITH CLDN4, AND
MUTAGENESIS OF LYS-646.
PubMed=16236711; DOI=10.1074/jbc.M503786200;
Tanaka M., Kamata R., Sakai R.;
"EphA2 phosphorylates the cytoplasmic tail of Claudin-4 and mediates
paracellular permeability.";
J. Biol. Chem. 280:42375-42382(2005).
[11]
TISSUE SPECIFICITY.
PubMed=17332925;
Liu D.-P., Wang Y., Koeffler H.P., Xie D.;
"Ephrin-A1 is a negative regulator in glioma through down-regulation
of EphA2 and FAK.";
Int. J. Oncol. 30:865-871(2007).
[12]
INTERACTION WITH INPPL1.
PubMed=17135240; DOI=10.1074/jbc.M608509200;
Zhuang G., Hunter S., Hwang Y., Chen J.;
"Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase
via phosphatidylinositol 3-Kinase-dependent Rac1 activation.";
J. Biol. Chem. 282:2683-2694(2007).
[13]
FUNCTION IN APOPTOSIS, AND INDUCTION BY UV.
PubMed=18339848; DOI=10.1158/0008-5472.CAN-07-2372;
Zhang G., Njauw C.-N., Park J.M., Naruse C., Asano M., Tsao H.;
"EphA2 is an essential mediator of UV radiation-induced apoptosis.";
Cancer Res. 68:1691-1696(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-579 AND
THR-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=18794797; DOI=10.1038/onc.2008.328;
Wykosky J., Palma E., Gibo D.M., Ringler S., Turner C.P., Debinski W.;
"Soluble monomeric EphrinA1 is released from tumor cells and is a
functional ligand for the EphA2 receptor.";
Oncogene 27:7260-7273(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-892 AND
SER-901, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
DISEASE, FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION, MUTAGENESIS
OF ASP-739 AND SER-897, AND PHOSPHORYLATION AT SER-897 BY PKB.
PubMed=19573808; DOI=10.1016/j.ccr.2009.04.009;
Miao H., Li D.Q., Mukherjee A., Guo H., Petty A., Cutter J.,
Basilion J.P., Sedor J., Wu J., Danielpour D., Sloan A.E., Cohen M.L.,
Wang B.;
"EphA2 mediates ligand-dependent inhibition and ligand-independent
promotion of cell migration and invasion via a reciprocal regulatory
loop with Akt.";
Cancer Cell 16:9-20(2009).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-435.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[19]
UBIQUITINATION BY STUB1.
PubMed=19567782; DOI=10.1158/1541-7786.MCR-08-0582;
Annamalai B., Liu X., Gopal U., Isaacs J.S.;
"Hsp90 is an essential regulator of EphA2 receptor stability and
signaling: implications for cancer cell migration and metastasis.";
Mol. Cancer Res. 7:1021-1032(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; TYR-628; THR-647
AND SER-869, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
FUNCTION IN CELL MIGRATION, AND INTERACTION WITH ARHGEF16; DOCK4 AND
ELMO2.
PubMed=20679435; DOI=10.1083/jcb.201005141;
Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S.,
Negishi M., Katoh H.;
"Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent
mechanism.";
J. Cell Biol. 190:461-477(2010).
[22]
FUNCTION IN KERATINOCYTE ADHESION AND DIFFERENTIATION, AND SUBCELLULAR
LOCATION.
PubMed=20861311; DOI=10.1091/mbc.E10-03-0242;
Lin S., Gordon K., Kaplan N., Getsios S.;
"Ligand targeting of EphA2 enhances keratinocyte adhesion and
differentiation via desmoglein 1.";
Mol. Biol. Cell 21:3902-3914(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
SUBCELLULAR LOCATION.
PubMed=20223987; DOI=10.1126/science.1181729;
Salaita K., Nair P.M., Petit R.S., Neve R.M., Das D., Gray J.W.,
Groves J.T.;
"Restriction of receptor movement alters cellular response: physical
force sensing by EphA2.";
Science 327:1380-1385(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
FUNCTION (MICROBIAL INFECTION).
PubMed=21516087; DOI=10.1038/nm.2341;
Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L.,
Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B.,
Zahid M.N., Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M.,
Pietschmann T., Patel A.H., Pessaux P., Doffoel M., Raffelsberger W.,
Poch O., McKeating J.A., Brino L., Baumert T.F.;
"EGFR and EphA2 are host factors for hepatitis C virus entry and
possible targets for antiviral therapy.";
Nat. Med. 17:589-595(2011).
[27]
INTERACTION WITH ANKS1A.
PubMed=22332920; DOI=10.1021/bi300141h;
Mercurio F.A., Marasco D., Pirone L., Pedone E.M., Pellecchia M.,
Leone M.;
"Solution structure of the first Sam domain of Odin and binding
studies with the EphA2 receptor.";
Biochemistry 51:2136-2145(2012).
[28]
INTERACTION WITH HHV-8 GLYCOPROTEIN L/GLYCOPROTEIN H (MICROBIAL
INFECTION).
PubMed=22635007; DOI=10.1038/nm.2805;
Hahn A.S., Kaufmann J.K., Wies E., Naschberger E., Panteleev-Ivlev J.,
Schmidt K., Holzer A., Schmidt M., Chen J., Konig S., Ensser A.,
Myoung J., Brockmeyer N.H., Sturzl M., Fleckenstein B., Neipel F.;
"The ephrin receptor tyrosine kinase A2 is a cellular receptor for
Kaposi's sarcoma-associated herpesvirus.";
Nat. Med. 18:961-966(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-575; SER-892; SER-897
AND SER-901, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
FUNCTION IN CELL MIGRATION, PHOSPHORYLATION AT TYR-930,
DEPHOSPHORYLATION AT TYR-930 BY PTPRF, AND INTERACTION WITH NCK1.
PubMed=23358419; DOI=10.1128/MCB.01708-12;
Lee H., Bennett A.M.;
"Receptor protein tyrosine phosphatase-receptor tyrosine kinase
substrate screen identifies EphA2 as a target for LAR in cell
migration.";
Mol. Cell. Biol. 33:1430-1441(2013).
[31]
INTERACTION WITH CEMIP.
PubMed=23936024; DOI=10.1371/journal.pone.0069473;
Tiwari A., Schneider M., Fiorino A., Haider R., Okoniewski M.J.,
Roschitzki B., Uzozie A., Menigatti M., Jiricny J., Marra G.;
"Early insights into the function of KIAA1199, a markedly
overexpressed protein in human colorectal tumors.";
PLoS ONE 8:E69473-E69473(2013).
[32]
PHOSPHORYLATION AT SER-897 BY RPS6KA1 AND RPS6KA3, AND FUNCTION IN
CELL MIGRATION.
PubMed=26158630; DOI=10.1038/ncomms8679;
Zhou Y., Yamada N., Tanaka T., Hori T., Yokoyama S., Hayakawa Y.,
Yano S., Fukuoka J., Koizumi K., Saiki I., Sakurai H.;
"Crucial roles of RSK in cell motility by catalysing serine
phosphorylation of EphA2.";
Nat. Commun. 6:7679-7679(2015).
[33]
PHOSPHORYLATION AT SER-897 BY PKA, PHOSPHORYLATION AT SER-901, AND
FUNCTION.
PubMed=27385333; DOI=10.1091/mbc.E16-01-0048;
Barquilla A., Lamberto I., Noberini R., Heynen-Genel S., Brill L.M.,
Pasquale E.B.;
"Protein kinase A can block EphA2 receptor-mediated cell repulsion by
increasing EphA2 S897 phosphorylation.";
Mol. Biol. Cell 27:2757-2770(2016).
[34]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 596-900.
PubMed=12467573; DOI=10.1016/S0969-2126(02)00907-3;
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.;
"Structures of the cancer-related Aurora-A, FAK, and EphA2 protein
kinases from nanovolume crystallography.";
Structure 10:1659-1667(2002).
[35]
STRUCTURE BY NMR OF 902-976.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the C-terminal SAM-domain of EPHAA2: ephrin
type-A receptor 2 precursor (EC 2.7.10.1).";
Submitted (JAN-2008) to the PDB data bank.
[36]
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, AND MUTAGENESIS OF ARG-103.
PubMed=19525919; DOI=10.1038/embor.2009.91;
Himanen J.P., Goldgur Y., Miao H., Myshkin E., Guo H., Buck M.,
Nguyen M., Rajashankar K.R., Wang B., Nikolov D.B.;
"Ligand recognition by A-class Eph receptors: crystal structures of
the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex.";
EMBO Rep. 10:722-728(2009).
[37]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 25-202, AND DISULFIDE BOND.
Structural genomics consortium (SGC);
"Ephrin A1 bound to the ligand binding domain of the human ephrin A2
(EPHA2) receptor protein kinase.";
Submitted (FEB-2009) to the PDB data bank.
[38]
STRUCTURE BY NMR OF 523-563.
Mayzel M.L., Bocharov E.V., Volynsky P.E., Arseniev A.S.;
"Left-handed dimer of EPHA2 transmembrane domain helix packing
diversity among receptor tyrosine kinases.";
Submitted (AUG-2009) to the PDB data bank.
[39]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 23-202 IN COMPLEX WITH
EFNA1, AND SUBUNIT.
PubMed=20505120; DOI=10.1073/pnas.1004148107;
Himanen J.P., Yermekbayeva L., Janes P.W., Walker J.R., Xu K.,
Atapattu L., Rajashankar K.R., Mensinga A., Lackmann M., Nikolov D.B.,
Dhe-Paganon S.;
"Architecture of Eph receptor clusters.";
Proc. Natl. Acad. Sci. U.S.A. 107:10860-10865(2010).
[40]
VARIANTS [LARGE SCALE ANALYSIS] ARG-391; MET-511; HIS-568; SER-777 AND
HIS-876.
PubMed=17344846; DOI=10.1038/nature05610;
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., 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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[41]
VARIANT CTRCT6 TRP-948.
PubMed=19005574;
Shiels A., Bennett T.M., Knopf H.L.S., Maraini G., Li A., Jiao X.,
Hejtmancik J.F.;
"The EPHA2 gene is associated with cataracts linked to chromosome
1p.";
Mol. Vis. 14:2042-2055(2008).
[42]
VARIANT CTRCT6 ILE-940.
PubMed=19306328; DOI=10.1002/humu.20995;
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.;
"Mutations of the EPHA2 receptor tyrosine kinase gene cause autosomal
dominant congenital cataract.";
Hum. Mutat. 30:E603-E611(2009).
[43]
VARIANT CTRCT6 GLN-721, AND CHARACTERIZATION OF VARIANT CTRCT6
GLN-721.
PubMed=19649315; DOI=10.1371/journal.pgen.1000584;
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.,
Elston R.C., Iyengar S.K., Wang B.;
"EPHA2 is associated with age-related cortical cataract in mice and
humans.";
PLoS Genet. 5:E1000584-E1000584(2009).
[44]
CHARACTERIZATION OF VARIANTS CTRCT6 ILE-940 AND CTRCT6 TRP-948.
PubMed=22570727; DOI=10.1371/journal.pone.0036564;
Park J.E., Son A.I., Hua R., Wang L., Zhang X., Zhou R.;
"Human cataract mutations in EPHA2 SAM domain alter receptor stability
and function.";
PLoS ONE 7:E36564-E36564(2012).
-!- 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. {ECO:0000269|PubMed:10655584,
ECO:0000269|PubMed:16236711, ECO:0000269|PubMed:18339848,
ECO:0000269|PubMed:19573808, ECO:0000269|PubMed:20679435,
ECO:0000269|PubMed:20861311, ECO:0000269|PubMed:23358419,
ECO:0000269|PubMed:26158630, ECO:0000269|PubMed:27385333}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
virus (HCV) in hepatocytes and facilitates its cell entry.
Mediates HCV entry by promoting the formation of the CD81-CLDN1
receptor complexes that are essential for HCV entry and by
enhancing membrane fusion of cells expressing HCV envelope
glycoproteins. {ECO:0000269|PubMed:21516087}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:2174105}.
-!- SUBUNIT: Homodimer. Interacts with SLA. Interacts (phosphorylated
form) with VAV2, VAV3 and PI3-kinase p85 subunit (PIK3R1, PIK3R2
or PIK3R3); critical for the EFNA1-induced activation of RAC1
which stimulates cell migration (By similarity). Interacts with
INPPL1; regulates activated EPHA2 endocytosis and degradation.
Interacts (inactivated form) with PTK2/FAK1 and interacts (EFNA1
ligand-activated form) with PTPN11; regulates integrin-mediated
adhesion. Interacts with ARHGEF16, DOCK4 and ELMO2; mediates
ligand-independent activation of RAC1 which stimulates cell
migration. Interacts with CLDN4; phosphorylates CLDN4 and may
regulate tight junctions. Interacts with ACP1. Interacts (via SAM
domain) with ANKS1A (via SAM domain). Interacts with CEMIP.
Interacts with NCK1; may regulate EPHA2 activity in cell migration
and adhesion. {ECO:0000250|UniProtKB:Q03145,
ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:12167657,
ECO:0000269|PubMed:16236711, ECO:0000269|PubMed:17135240,
ECO:0000269|PubMed:19525919, ECO:0000269|PubMed:20505120,
ECO:0000269|PubMed:20679435, ECO:0000269|PubMed:22332920,
ECO:0000269|PubMed:23358419, ECO:0000269|PubMed:23936024}.
-!- SUBUNIT: (Microbial infection) Interacts with human herpes virus
8/HHV-8 glycoprotein L/gL and glycoprotein H/gH heterodimer; this
interaction triggers EPHA2 phosphorylation and endocytosis,
allowing virus entry. {ECO:0000269|PubMed:22635007}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=2; IntAct=EBI-702104, EBI-491549;
P20827:EFNA1; NbExp=9; IntAct=EBI-702104, EBI-715194;
P52803:EFNA5; NbExp=6; IntAct=EBI-702104, EBI-1753674;
Q15375:EPHA7; NbExp=3; IntAct=EBI-702104, EBI-1383428;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-702104, EBI-352572;
O15357-1:INPPL1; NbExp=3; IntAct=EBI-702104, EBI-15963021;
Q05397:PTK2; NbExp=3; IntAct=EBI-702104, EBI-702142;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18794797,
ECO:0000269|PubMed:19573808, ECO:0000269|PubMed:20223987,
ECO:0000269|PubMed:20861311}; Single-pass type I membrane protein
{ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000269|PubMed:19573808}; Single-pass type I membrane protein
{ECO:0000255}. Cell projection, lamellipodium membrane
{ECO:0000269|PubMed:19573808}; Single-pass type I membrane protein
{ECO:0000255}. Cell junction, focal adhesion
{ECO:0000269|PubMed:10655584}. Note=Present at regions of cell-
cell contacts but also at the leading edge of migrating cells
(PubMed:19573808, PubMed:20861311). Relocates from the plasma
membrane to the cytoplasmic and perinuclear regions in cancer
cells (PubMed:18794797). {ECO:0000269|PubMed:18794797,
ECO:0000269|PubMed:19573808, ECO:0000269|PubMed:20861311,
ECO:0000269|PubMed:26158630}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P29317-1; Sequence=Displayed;
Name=2;
IsoId=P29317-2; Sequence=VSP_056014, VSP_056015;
-!- 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. {ECO:0000269|PubMed:17332925}.
-!- INDUCTION: Up-regulated by UV irradiation via a TP53-independent,
MAPK-dependent mechanism. {ECO:0000269|PubMed:18339848}.
-!- PTM: Autophosphorylates. Phosphorylated on tyrosine upon binding
and activation by EFNA1. 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 (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-
930 by PTPRF prevents the interaction of EPHA2 with NCK1.
Phosphorylated at Ser-897 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 at Ser-897 in response to TNF by RPS6KA1 and
RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell migration
(PubMed:26158630). Phosphorylated at Ser-897 by PKA; blocks cell
retraction induced by EPHA2 kinase activity (PubMed:27385333).
Dephosphorylated by ACP1. {ECO:0000269|PubMed:10655584,
ECO:0000269|PubMed:18794797, ECO:0000269|PubMed:19573808,
ECO:0000269|PubMed:23358419, ECO:0000269|PubMed:26158630,
ECO:0000269|PubMed:27385333}.
-!- 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 (By similarity). {ECO:0000250}.
-!- DISEASE: Cataract 6, multiple types (CTRCT6) [MIM:116600]: An
opacification of the crystalline lens of the eye that frequently
results in visual impairment or blindness. Opacities vary in
morphology, are often confined to a portion of the lens, and may
be static or progressive. CTRCT6 includes posterior polar and age-
related cortical cataracts, among others. Posterior polar cataract
is a subcapsular opacity, usually disk-shaped, located at the back
of the lens. Age-related cortical cataract is a developmental
punctate opacity restricted to the cortex. The cataract is white
or cerulean, increases in number with age, but rarely affects
vision. {ECO:0000269|PubMed:19005574, ECO:0000269|PubMed:19306328,
ECO:0000269|PubMed:19649315, ECO:0000269|PubMed:22570727}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Overexpressed in several cancer types and promotes
malignancy. {ECO:0000269|PubMed:19573808}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/EPHA2ID40462ch1p36.html";
-----------------------------------------------------------------------
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EMBL; M59371; AAA53375.1; -; mRNA.
EMBL; EU826606; ACF47642.1; -; mRNA.
EMBL; AL451042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471167; EAW51769.1; -; Genomic_DNA.
EMBL; BC037166; AAH37166.1; -; mRNA.
CCDS; CCDS169.1; -. [P29317-1]
PIR; A36355; A36355.
RefSeq; NP_004422.2; NM_004431.4. [P29317-1]
UniGene; Hs.171596; -.
PDB; 1MQB; X-ray; 2.30 A; A/B=596-900.
PDB; 2E8N; NMR; -; A=902-976.
PDB; 2K9Y; NMR; -; A/B=523-563.
PDB; 2KSO; NMR; -; A=908-972.
PDB; 2X10; X-ray; 3.00 A; A=27-534.
PDB; 2X11; X-ray; 4.83 A; A=27-534.
PDB; 3C8X; X-ray; 1.95 A; A=23-202.
PDB; 3CZU; X-ray; 2.65 A; A=23-202.
PDB; 3FL7; X-ray; 2.50 A; A=23-531.
PDB; 3HEI; X-ray; 2.00 A; A/C/E/G/I/K/M/O=28-201.
PDB; 3HPN; X-ray; 2.52 A; A/B/C/D/E/F=28-201.
PDB; 3KKA; X-ray; 2.40 A; C/D/E=903-971.
PDB; 3MBW; X-ray; 2.81 A; A=23-326.
PDB; 3MX0; X-ray; 3.51 A; A/C=27-435.
PDB; 3SKJ; X-ray; 2.50 A; E/F=23-202.
PDB; 4P2K; X-ray; 1.50 A; A=590-876.
PDB; 4PDO; X-ray; 2.10 A; A/B=590-876.
PDB; 4TRL; X-ray; 2.45 A; A=590-876.
PDB; 5EK7; X-ray; 1.90 A; A/B=583-876.
PDB; 5I9U; X-ray; 1.89 A; A=596-900.
PDB; 5I9V; X-ray; 1.46 A; A=596-900.
PDB; 5I9W; X-ray; 1.36 A; A=596-900.
PDB; 5I9X; X-ray; 1.43 A; A=596-900.
PDB; 5I9Y; X-ray; 1.23 A; A=596-900.
PDB; 5I9Z; X-ray; 1.70 A; A=596-900.
PDB; 5IA0; X-ray; 1.95 A; A/B/C=596-900.
PDB; 5IA1; X-ray; 2.04 A; A=596-900.
PDB; 5IA2; X-ray; 1.62 A; A=596-900.
PDB; 5IA3; X-ray; 1.79 A; A=596-900.
PDB; 5IA4; X-ray; 1.80 A; A=596-900.
PDB; 5IA5; X-ray; 1.78 A; A=596-900.
PDB; 5NJZ; X-ray; 1.77 A; A=596-900.
PDB; 5NK0; X-ray; 1.60 A; A=596-900.
PDB; 5NK1; X-ray; 1.55 A; A=596-900.
PDB; 5NK2; X-ray; 1.65 A; A=596-900.
PDB; 5NK3; X-ray; 1.59 A; A=596-900.
PDB; 5NK4; X-ray; 1.45 A; A=596-900.
PDB; 5NK5; X-ray; 1.33 A; A=596-900.
PDB; 5NK6; X-ray; 1.27 A; A=596-900.
PDB; 5NK7; X-ray; 1.89 A; A=596-900.
PDB; 5NK8; X-ray; 1.76 A; A=596-900.
PDB; 5NK9; X-ray; 1.59 A; A=596-900.
PDB; 5NKA; X-ray; 1.38 A; A=596-900.
PDB; 5NKB; X-ray; 1.50 A; A=596-900.
PDB; 5NKC; X-ray; 1.45 A; A=596-900.
PDB; 5NKD; X-ray; 1.41 A; A=596-900.
PDB; 5NKE; X-ray; 1.39 A; A=596-900.
PDB; 5NKF; X-ray; 1.10 A; A=596-900.
PDB; 5NKG; X-ray; 1.10 A; A=596-900.
PDB; 5NKH; X-ray; 1.29 A; A=596-900.
PDB; 5NKI; X-ray; 1.68 A; A=596-900.
PDB; 5NZ9; NMR; -; A=945-969.
PDBsum; 1MQB; -.
PDBsum; 2E8N; -.
PDBsum; 2K9Y; -.
PDBsum; 2KSO; -.
PDBsum; 2X10; -.
PDBsum; 2X11; -.
PDBsum; 3C8X; -.
PDBsum; 3CZU; -.
PDBsum; 3FL7; -.
PDBsum; 3HEI; -.
PDBsum; 3HPN; -.
PDBsum; 3KKA; -.
PDBsum; 3MBW; -.
PDBsum; 3MX0; -.
PDBsum; 3SKJ; -.
PDBsum; 4P2K; -.
PDBsum; 4PDO; -.
PDBsum; 4TRL; -.
PDBsum; 5EK7; -.
PDBsum; 5I9U; -.
PDBsum; 5I9V; -.
PDBsum; 5I9W; -.
PDBsum; 5I9X; -.
PDBsum; 5I9Y; -.
PDBsum; 5I9Z; -.
PDBsum; 5IA0; -.
PDBsum; 5IA1; -.
PDBsum; 5IA2; -.
PDBsum; 5IA3; -.
PDBsum; 5IA4; -.
PDBsum; 5IA5; -.
PDBsum; 5NJZ; -.
PDBsum; 5NK0; -.
PDBsum; 5NK1; -.
PDBsum; 5NK2; -.
PDBsum; 5NK3; -.
PDBsum; 5NK4; -.
PDBsum; 5NK5; -.
PDBsum; 5NK6; -.
PDBsum; 5NK7; -.
PDBsum; 5NK8; -.
PDBsum; 5NK9; -.
PDBsum; 5NKA; -.
PDBsum; 5NKB; -.
PDBsum; 5NKC; -.
PDBsum; 5NKD; -.
PDBsum; 5NKE; -.
PDBsum; 5NKF; -.
PDBsum; 5NKG; -.
PDBsum; 5NKH; -.
PDBsum; 5NKI; -.
PDBsum; 5NZ9; -.
ProteinModelPortal; P29317; -.
SMR; P29317; -.
BioGrid; 108288; 83.
CORUM; P29317; -.
DIP; DIP-96N; -.
IntAct; P29317; 38.
MINT; P29317; -.
STRING; 9606.ENSP00000351209; -.
BindingDB; P29317; -.
ChEMBL; CHEMBL2068; -.
DrugBank; DB01254; Dasatinib.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB08896; Regorafenib.
GuidetoPHARMACOLOGY; 1822; -.
GlyConnect; 777; -.
iPTMnet; P29317; -.
PhosphoSitePlus; P29317; -.
SwissPalm; P29317; -.
UniCarbKB; P29317; -.
BioMuta; EPHA2; -.
DMDM; 229462861; -.
EPD; P29317; -.
MaxQB; P29317; -.
PaxDb; P29317; -.
PeptideAtlas; P29317; -.
PRIDE; P29317; -.
ProteomicsDB; 54535; -.
DNASU; 1969; -.
Ensembl; ENST00000358432; ENSP00000351209; ENSG00000142627. [P29317-1]
GeneID; 1969; -.
KEGG; hsa:1969; -.
UCSC; uc001aya.2; human. [P29317-1]
CTD; 1969; -.
DisGeNET; 1969; -.
EuPathDB; HostDB:ENSG00000142627.12; -.
GeneCards; EPHA2; -.
HGNC; HGNC:3386; EPHA2.
HPA; CAB010464; -.
MalaCards; EPHA2; -.
MIM; 116600; phenotype.
MIM; 176946; gene.
neXtProt; NX_P29317; -.
OpenTargets; ENSG00000142627; -.
Orphanet; 98993; Posterior polar cataract.
Orphanet; 98994; Total congenital cataract.
PharmGKB; PA27818; -.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00910000144084; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; P29317; -.
KO; K05103; -.
OMA; CSPGFFK; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; P29317; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; P29317; -.
SIGNOR; P29317; -.
ChiTaRS; EPHA2; human.
EvolutionaryTrace; P29317; -.
GeneWiki; EPH_receptor_A2; -.
GenomeRNAi; 1969; -.
PRO; PR:P29317; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000142627; Expressed in 168 organ(s), highest expression level in ectocervix.
CleanEx; HS_EPHA2; -.
ExpressionAtlas; P29317; baseline and differential.
Genevisible; P29317; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0031256; C:leading edge membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
GO; GO:0048320; P:axial mesoderm formation; IEA:Ensembl.
GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
GO; GO:0046849; P:bone remodeling; ISS:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; ISS:UniProtKB.
GO; GO:0046058; P:cAMP metabolic process; IMP:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0048870; P:cell motility; IMP:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:UniProtKB.
GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0070309; P:lens fiber cell morphogenesis; ISS:UniProtKB.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
GO; GO:0032682; P:negative regulation of chemokine production; IEA:Ensembl.
GO; GO:1901491; P:negative regulation of lymphangiogenesis; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0021915; P:neural tube development; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0060035; P:notochord cell development; IEA:Ensembl.
GO; GO:0014028; P:notochord formation; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; ISS:UniProtKB.
GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB.
GO; GO:1904238; P:pericyte cell differentiation; IEA:Ensembl.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
GO; GO:0043491; P:protein kinase B signaling; IDA:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:UniProtKB.
GO; GO:0070848; P:response to growth factor; IMP:UniProtKB.
GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
CDD; cd10480; EphR_LBD_A2; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034263; EphA2_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Angiogenesis; Apoptosis;
ATP-binding; Cataract; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Complete proteome; Differentiation; Disease mutation;
Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 976 Ephrin type-A receptor 2.
/FTId=PRO_0000016800.
TOPO_DOM 24 537 Extracellular. {ECO:0000255}.
TRANSMEM 538 558 Helical. {ECO:0000255}.
TOPO_DOM 559 976 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 206 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 328 432 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 438 529 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 613 875 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 904 968 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 619 627 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 206 Mediates interaction with CLDN4.
{ECO:0000269|PubMed:16236711}.
REGION 606 906 Mediates interaction with ARHGEF16 and
ELMO2. {ECO:0000269|PubMed:20679435}.
REGION 886 976 Negatively regulates interaction with
ARHGEF16. {ECO:0000269|PubMed:20679435}.
MOTIF 974 976 PDZ-binding. {ECO:0000255}.
COMPBIAS 188 325 Cys-rich.
ACT_SITE 739 739 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 646 646 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 575 575 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 579 579 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 588 588 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 594 594 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q03145}.
MOD_RES 628 628 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 647 647 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 735 735 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q03145}.
MOD_RES 772 772 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q03145}.
MOD_RES 869 869 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 897 897 Phosphoserine; by PKB/AKT1, RPS6KA1,
RPS6KA3 AND PKA.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19573808,
ECO:0000269|PubMed:26158630,
ECO:0000269|PubMed:27385333}.
MOD_RES 901 901 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:27385333}.
MOD_RES 921 921 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 930 930 Phosphotyrosine.
{ECO:0000269|PubMed:23358419}.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 435 435 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 70 188
DISULFID 105 115
VAR_SEQ 477 497 GDSNSYNVRRTEGFSVTLDDL -> VTPRGAGLALAGPTAG
DRLVT (in isoform 2).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_056014.
VAR_SEQ 498 976 Missing (in isoform 2).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_056015.
VARIANT 99 99 K -> N (in dbSNP:rs1058372).
/FTId=VAR_055989.
VARIANT 391 391 G -> R (in dbSNP:rs34192549).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042121.
VARIANT 511 511 T -> M (in dbSNP:rs55747232).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042122.
VARIANT 568 568 R -> H (in dbSNP:rs56198600).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042123.
VARIANT 631 631 M -> T (in dbSNP:rs34021505).
/FTId=VAR_055990.
VARIANT 721 721 R -> Q (in CTRCT6; retained in the
cytoplasm and constitutively active it
alters EPHA2 signaling;
dbSNP:rs116506614).
{ECO:0000269|PubMed:19649315}.
/FTId=VAR_062532.
VARIANT 777 777 G -> S (in a gastric adenocarcinoma
sample; somatic mutation;
dbSNP:rs922655349).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042124.
VARIANT 876 876 R -> H (in dbSNP:rs35903225).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042125.
VARIANT 940 940 T -> I (in CTRCT6; reduced protein
stability and reduced ability to
stimulate cell migration in absence of
its ephrin ligand; dbSNP:rs137853200).
{ECO:0000269|PubMed:19306328,
ECO:0000269|PubMed:22570727}.
/FTId=VAR_058907.
VARIANT 948 948 G -> W (in CTRCT6; reduced protein
stability and reduced ability to
stimulate cell migration in absence of
its ephrin ligand; dbSNP:rs137853199).
{ECO:0000269|PubMed:19005574,
ECO:0000269|PubMed:22570727}.
/FTId=VAR_058908.
MUTAGEN 103 103 R->E: Significantly reduced response to
EFNA1. {ECO:0000269|PubMed:19525919}.
MUTAGEN 646 646 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:16236711}.
MUTAGEN 739 739 D->N: Increases serum-induced chemotaxis.
Loss of EFNA1-dependent regulation of
cell migration.
{ECO:0000269|PubMed:19573808}.
MUTAGEN 897 897 S->A,D: Loss of serum-induced
phosphorylation by PKB. Loss of serum-
induced chemotaxis.
{ECO:0000269|PubMed:19573808}.
CONFLICT 94 99 IFIELK -> NNFELN (in Ref. 1; AAA53375).
{ECO:0000305}.
STRAND 28 33 {ECO:0000244|PDB:3C8X}.
HELIX 34 36 {ECO:0000244|PDB:3C8X}.
TURN 37 40 {ECO:0000244|PDB:3HPN}.
STRAND 44 57 {ECO:0000244|PDB:3C8X}.
STRAND 59 62 {ECO:0000244|PDB:3C8X}.
STRAND 64 69 {ECO:0000244|PDB:3C8X}.
STRAND 73 76 {ECO:0000244|PDB:3C8X}.
STRAND 79 82 {ECO:0000244|PDB:3C8X}.
STRAND 92 103 {ECO:0000244|PDB:3C8X}.
HELIX 105 107 {ECO:0000244|PDB:3C8X}.
STRAND 108 110 {ECO:0000244|PDB:3HEI}.
TURN 112 114 {ECO:0000244|PDB:3SKJ}.
STRAND 119 128 {ECO:0000244|PDB:3C8X}.
HELIX 136 138 {ECO:0000244|PDB:3C8X}.
STRAND 139 145 {ECO:0000244|PDB:3C8X}.
STRAND 148 151 {ECO:0000244|PDB:3MBW}.
HELIX 153 157 {ECO:0000244|PDB:3HEI}.
STRAND 161 170 {ECO:0000244|PDB:3C8X}.
STRAND 175 187 {ECO:0000244|PDB:3C8X}.
STRAND 189 199 {ECO:0000244|PDB:3C8X}.
STRAND 204 206 {ECO:0000244|PDB:3FL7}.
STRAND 209 211 {ECO:0000244|PDB:3FL7}.
STRAND 218 221 {ECO:0000244|PDB:3MBW}.
STRAND 224 227 {ECO:0000244|PDB:3FL7}.
STRAND 238 240 {ECO:0000244|PDB:3MBW}.
STRAND 244 247 {ECO:0000244|PDB:3FL7}.
STRAND 253 257 {ECO:0000244|PDB:3MBW}.
STRAND 266 269 {ECO:0000244|PDB:3FL7}.
STRAND 272 275 {ECO:0000244|PDB:3FL7}.
STRAND 286 288 {ECO:0000244|PDB:3MBW}.
STRAND 295 298 {ECO:0000244|PDB:3FL7}.
STRAND 335 338 {ECO:0000244|PDB:3FL7}.
STRAND 343 348 {ECO:0000244|PDB:3FL7}.
STRAND 361 369 {ECO:0000244|PDB:3FL7}.
STRAND 376 378 {ECO:0000244|PDB:3FL7}.
STRAND 384 387 {ECO:0000244|PDB:3FL7}.
STRAND 389 392 {ECO:0000244|PDB:3FL7}.
STRAND 394 400 {ECO:0000244|PDB:3FL7}.
STRAND 407 415 {ECO:0000244|PDB:3FL7}.
HELIX 419 421 {ECO:0000244|PDB:3FL7}.
STRAND 427 433 {ECO:0000244|PDB:3FL7}.
STRAND 441 446 {ECO:0000244|PDB:3FL7}.
STRAND 453 457 {ECO:0000244|PDB:3FL7}.
TURN 460 465 {ECO:0000244|PDB:3FL7}.
STRAND 467 475 {ECO:0000244|PDB:3FL7}.
STRAND 483 493 {ECO:0000244|PDB:3FL7}.
STRAND 502 510 {ECO:0000244|PDB:3FL7}.
STRAND 522 525 {ECO:0000244|PDB:3FL7}.
HELIX 536 556 {ECO:0000244|PDB:2K9Y}.
STRAND 557 561 {ECO:0000244|PDB:2K9Y}.
HELIX 591 594 {ECO:0000244|PDB:5EK7}.
HELIX 597 600 {ECO:0000244|PDB:4PDO}.
HELIX 601 604 {ECO:0000244|PDB:5I9Y}.
HELIX 610 612 {ECO:0000244|PDB:5NKF}.
STRAND 613 621 {ECO:0000244|PDB:5NKF}.
STRAND 623 625 {ECO:0000244|PDB:5I9V}.
STRAND 626 632 {ECO:0000244|PDB:5NKF}.
HELIX 635 637 {ECO:0000244|PDB:5NKH}.
STRAND 641 648 {ECO:0000244|PDB:5NKF}.
HELIX 654 668 {ECO:0000244|PDB:5NKF}.
STRAND 678 682 {ECO:0000244|PDB:5NKF}.
STRAND 684 693 {ECO:0000244|PDB:5NKF}.
HELIX 700 706 {ECO:0000244|PDB:5NKF}.
TURN 707 709 {ECO:0000244|PDB:5I9Y}.
HELIX 713 732 {ECO:0000244|PDB:5NKF}.
HELIX 742 744 {ECO:0000244|PDB:5NKF}.
STRAND 745 747 {ECO:0000244|PDB:5NKF}.
STRAND 753 755 {ECO:0000244|PDB:5NKF}.
HELIX 762 766 {ECO:0000244|PDB:5NKF}.
STRAND 770 772 {ECO:0000244|PDB:5NKF}.
STRAND 776 778 {ECO:0000244|PDB:5NKH}.
HELIX 781 783 {ECO:0000244|PDB:5NKF}.
HELIX 786 791 {ECO:0000244|PDB:5NKF}.
HELIX 796 811 {ECO:0000244|PDB:5NKF}.
TURN 817 820 {ECO:0000244|PDB:5NKF}.
HELIX 823 831 {ECO:0000244|PDB:5NKF}.
HELIX 844 853 {ECO:0000244|PDB:5NKF}.
HELIX 858 860 {ECO:0000244|PDB:5NKF}.
HELIX 864 876 {ECO:0000244|PDB:5NKF}.
HELIX 878 882 {ECO:0000244|PDB:5NKF}.
HELIX 884 887 {ECO:0000244|PDB:5IA0}.
HELIX 909 915 {ECO:0000244|PDB:3KKA}.
HELIX 919 921 {ECO:0000244|PDB:3KKA}.
HELIX 922 927 {ECO:0000244|PDB:3KKA}.
HELIX 933 937 {ECO:0000244|PDB:3KKA}.
HELIX 941 946 {ECO:0000244|PDB:3KKA}.
HELIX 952 964 {ECO:0000244|PDB:3KKA}.
SEQUENCE 976 AA; 108266 MW; 845D7E1BBCCAACCC CRC64;
MELQAARACF ALLWGCALAA AAAAQGKEVV LLDFAAAGGE LGWLTHPYGK GWDLMQNIMN
DMPIYMYSVC NVMSGDQDNW LRTNWVYRGE AERIFIELKF TVRDCNSFPG GASSCKETFN
LYYAESDLDY GTNFQKRLFT KIDTIAPDEI TVSSDFEARH VKLNVEERSV GPLTRKGFYL
AFQDIGACVA LLSVRVYYKK CPELLQGLAH FPETIAGSDA PSLATVAGTC VDHAVVPPGG
EEPRMHCAVD GEWLVPIGQC LCQAGYEKVE DACQACSPGF FKFEASESPC LECPEHTLPS
PEGATSCECE EGFFRAPQDP ASMPCTRPPS APHYLTAVGM GAKVELRWTP PQDSGGREDI
VYSVTCEQCW PESGECGPCE ASVRYSEPPH GLTRTSVTVS DLEPHMNYTF TVEARNGVSG
LVTSRSFRTA SVSINQTEPP KVRLEGRSTT SLSVSWSIPP PQQSRVWKYE VTYRKKGDSN
SYNVRRTEGF SVTLDDLAPD TTYLVQVQAL TQEGQGAGSK VHEFQTLSPE GSGNLAVIGG
VAVGVVLLLV LAGVGFFIHR RRKNQRARQS PEDVYFSKSE QLKPLKTYVD PHTYEDPNQA
VLKFTTEIHP SCVTRQKVIG AGEFGEVYKG MLKTSSGKKE VPVAIKTLKA GYTEKQRVDF
LGEAGIMGQF SHHNIIRLEG VISKYKPMMI ITEYMENGAL DKFLREKDGE FSVLQLVGML
RGIAAGMKYL ANMNYVHRDL AARNILVNSN LVCKVSDFGL SRVLEDDPEA TYTTSGGKIP
IRWTAPEAIS YRKFTSASDV WSFGIVMWEV MTYGERPYWE LSNHEVMKAI NDGFRLPTPM
DCPSAIYQLM MQCWQQERAR RPKFADIVSI LDKLIRAPDS LKTLADFDPR VSIRLPSTSG
SEGVPFRTVS EWLESIKMQQ YTEHFMAAGY TAIEKVVQMT NDDIKRIGVR LPGHQKRIAY
SLLGLKDQVN TVGIPI


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