Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK) (Tyrosine-protein kinase receptor MPK-5) (Tyrosine-protein kinase receptor SEK-2)

 EPHA2_MOUSE             Reviewed;         977 AA.
Q03145; Q3UNI2; Q60633; Q62212;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 183.
RecName: Full=Ephrin type-A receptor 2;
EC=2.7.10.1;
AltName: Full=Epithelial cell kinase;
AltName: Full=Tyrosine-protein kinase receptor ECK;
AltName: Full=Tyrosine-protein kinase receptor MPK-5;
AltName: Full=Tyrosine-protein kinase receptor SEK-2;
Flags: Precursor;
Name=Epha2; Synonyms=Eck, Myk2, Sek2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, CATALYTIC ACTIVITY, AND
DEVELOPMENTAL STAGE.
PubMed=8183555;
Ganju P., Shigemoto K., Brennan J., Entwistle A., Reith A.D.;
"The Eck receptor tyrosine kinase is implicated in pattern formation
during gastrulation, hindbrain segmentation and limb development.";
Oncogene 9:1613-1624(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
PubMed=7918100; DOI=10.1016/0925-4773(94)90078-7;
Ruiz J.C., Robertson E.J.;
"The expression of the receptor-protein tyrosine kinase gene, eck, is
highly restricted during early mouse development.";
Mech. Dev. 46:87-100(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Vagina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 552-977, AND DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=7947319; DOI=10.1016/0925-4773(94)90091-4;
Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P.,
Nieto A., Wilkinson D.G., Charnay P., Gilardi P.;
"Several receptor tyrosine kinase genes of the Eph family are
segmentally expressed in the developing hindbrain.";
Mech. Dev. 47:3-17(1994).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 742-799.
TISSUE=Embryonic brain;
PubMed=1281307;
Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G.,
Chestier A., Wilkinson D.G., Charnay P.;
"An Eph-related receptor protein tyrosine kinase gene segmentally
expressed in the developing mouse hindbrain.";
Oncogene 7:2499-2506(1992).
[9]
INTERACTION WITH SLA.
TISSUE=Embryonic brain;
PubMed=7543898; DOI=10.1074/jbc.270.33.19201;
Pandey A., Duan H., Dixit V.M.;
"Characterization of a novel Src-like adapter protein that associates
with the Eck receptor tyrosine kinase.";
J. Biol. Chem. 270:19201-19204(1995).
[10]
DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=11287184; DOI=10.1016/S0925-4773(01)00290-8;
Naruse-Nakajima C., Asano M., Iwakura Y.;
"Involvement of EphA2 in the formation of the tail notochord via
interaction with ephrinA1.";
Mech. Dev. 102:95-105(2001).
[11]
FUNCTION IN ANGIOGENESIS, AND DISRUPTION PHENOTYPE.
PubMed=15054110; DOI=10.1242/jcs.01061;
Brantley-Sieders D.M., Caughron J., Hicks D., Pozzi A., Ruiz J.C.,
Chen J.;
"EphA2 receptor tyrosine kinase regulates endothelial cell migration
and vascular assembly through phosphoinositide 3-kinase-mediated Rac1
GTPase activation.";
J. Cell Sci. 117:2037-2049(2004).
[12]
FUNCTION IN CELL PROLIFERATION, AND DISRUPTION PHENOTYPE.
PubMed=16849550; DOI=10.1158/0008-5472.CAN-06-0004;
Guo H., Miao H., Gerber L., Singh J., Denning M.F., Gilliam A.C.,
Wang B.;
"Disruption of EphA2 receptor tyrosine kinase leads to increased
susceptibility to carcinogenesis in mouse skin.";
Cancer Res. 66:7050-7058(2006).
[13]
FUNCTION IN ANGIOGENESIS, INTERACTION WITH VAV2 AND VAV3, AND
MUTAGENESIS OF TYR-589; TYR-595 AND ASP-740.
PubMed=16782872; DOI=10.1128/MCB.02215-05;
Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W.,
Chen J.;
"Essential role of Vav family guanine nucleotide exchange factors in
EphA receptor-mediated angiogenesis.";
Mol. Cell. Biol. 26:4830-4842(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH VAV2;
VAV3 AND PI3-KINASE P85 SUBUNIT, PHOSPHORYLATION AT TYR-589; TYR-595;
TYR-736 AND TYR-773, AND MUTAGENESIS OF TYR-589; TYR-595; TYR-736;
TYR-773 AND TYR-931.
PubMed=18387945; DOI=10.1074/jbc.M709934200;
Fang W.B., Brantley-Sieders D.M., Hwang Y., Ham A.-J.L., Chen J.;
"Identification and functional analysis of phosphorylated tyrosine
residues within EphA2 receptor tyrosine kinase.";
J. Biol. Chem. 283:16017-16026(2008).
[15]
FUNCTION IN LENS FIBER CELLS MORPHOGENESIS.
PubMed=18948590; DOI=10.1073/pnas.0808987105;
Cooper M.A., Son A.I., Komlos D., Sun Y., Kleiman N.J., Zhou R.;
"Loss of ephrin-A5 function disrupts lens fiber cell packing and leads
to cataract.";
Proc. Natl. Acad. Sci. U.S.A. 105:16620-16625(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-595 AND TYR-773, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
FUNCTION IN BONE IN REMODELING.
PubMed=19299512; DOI=10.1074/jbc.M807598200;
Irie N., Takada Y., Watanabe Y., Matsuzaki Y., Naruse C., Asano M.,
Iwakura Y., Suda T., Matsuo K.;
"Bidirectional signaling through ephrinA2-EphA2 enhances
osteoclastogenesis and suppresses osteoblastogenesis.";
J. Biol. Chem. 284:14637-14644(2009).
[19]
FUNCTION IN MAMMARY GLAND DEVELOPMENT.
PubMed=19321667; DOI=10.1091/mbc.E08-04-0378;
Vaught D., Chen J., Brantley-Sieders D.M.;
"Regulation of mammary gland branching morphogenesis by EphA2 receptor
tyrosine kinase.";
Mol. Biol. Cell 20:2572-2581(2009).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-408 AND ASN-436.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-408 AND ASN-436.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[22]
UBIQUITINATION, AND INTERACTION WITH ANKS1A.
PubMed=20100865; DOI=10.1128/MCB.01605-09;
Kim J., Lee H., Kim Y., Yoo S., Park E., Park S.;
"The SAM domains of Anks family proteins are critically involved in
modulating the degradation of EphA receptors.";
Mol. Cell. Biol. 30:1582-1592(2010).
[23]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=27446912; DOI=10.3389/fcell.2016.00058;
Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J.,
de Reynies A., Aurade F., Chang T.H., Zammit P.S., Relaix F.;
"Gene expression profiling of muscle stem cells identifies novel
regulators of postnatal myogenesis.";
Front. Cell Dev. Biol. 4:58-58(2016).
-!- 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 signaling pathway. May also participate in UV radiation-
induced apoptosis and have a ligand-independent stimulatory effect
on chemotactic cell migration. During development, may function in
distinctive aspects of pattern formation and subsequently in
development of several fetal tissues. Involved for instance in
angiogenesis, in early hindbrain development and epithelial
proliferation and branching morphogenesis during mammary gland
development. Engaged by the ligand ephrin-A5/EFNA5 may regulate
lens fiber cells shape and interactions and be important for lens
transparency development and maintenance. With ephrin-A2/EFNA2 may
play a role in bone remodeling through regulation of
osteoclastogenesis and osteoblastogenesis.
{ECO:0000269|PubMed:15054110, ECO:0000269|PubMed:16782872,
ECO:0000269|PubMed:16849550, ECO:0000269|PubMed:18387945,
ECO:0000269|PubMed:18948590, ECO:0000269|PubMed:19299512,
ECO:0000269|PubMed:19321667}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:8183555}.
-!- SUBUNIT: Homodimer. 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 with CEMIP. Interacts with NCK1; may regulate
EPHA2 activity in cell migration and adhesion. 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. Interacts with
ANKS1A. {ECO:0000269|PubMed:16782872, ECO:0000269|PubMed:18387945,
ECO:0000269|PubMed:20100865, ECO:0000269|PubMed:7543898}.
-!- INTERACTION:
Q03137:Epha4; NbExp=3; IntAct=EBI-529701, EBI-1539152;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, lamellipodium membrane
{ECO:0000250|UniProtKB:P29317}; Single-pass type I membrane
protein {ECO:0000255}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:P29317}. Note=Present at regions of cell-
cell contacts but also at the leading edge of migrating cells.
Relocates from the plasma membrane to the cytoplasmic and
perinuclear regions in cancer cells.
{ECO:0000250|UniProtKB:P29317}.
-!- TISSUE SPECIFICITY: Expressed in the lung, intestine and liver
(PubMed:11287184). Expressed in myogenic progenitor cells
(PubMed:27446912). {ECO:0000269|PubMed:11287184,
ECO:0000269|PubMed:27446912}.
-!- DEVELOPMENTAL STAGE: First detected in gastrulation stage embryos
(6.5-7.5 dpc) in ectodermal cells adjacent to the distal region of
the primitive streak. By the neural plate stage (approximately 7.5
dpc), EPHA2 expression becomes restricted to the extreme distal
end or node of the primitive streak. After the beginning of
somitogenesis (approximately 8.0 dpc), expression persists in the
node as this structure regresses toward the caudal end of the
embryo. In addition, beginning at the mid head fold stage
(approximately 7.75 dpc), we observe that EPHA2 exhibits a dynamic
and spatially restricted expression pattern in the prospective
hindbrain region. EPHA2 transcripts are initially detected in a 5-
cell wide strip of mesodermal cells underlying prospective
rhombomere 4 (R4). Subsequently at the beginning of somitogenesis,
expression is observed in prospective R4. At the 4-8-somite stage,
EPHA2 transcripts are observed in R4, mesenchymal cells underlying
R4, and surface ectoderm in the vicinity of the developing second
branchial arch. By the 10-somite stage, expression in these cells
is down-regulated. Additionally, at the 5-8-somite stage, EPHA2
transcripts are detected initially in the lateral mesenchyme
immediately underlying the surface ectoderm adjacent to R5 and R6,
and subsequently in surface ectoderm overlying the developing
third branchial arch. In myogenic progenitor cells, expressed
during the acquisition of muscle stem cell properties, from E18.5
to adulthood (PubMed:27446912). {ECO:0000269|PubMed:11287184,
ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:7918100,
ECO:0000269|PubMed:7947319, ECO:0000269|PubMed:8183555}.
-!- PTM: Autophosphorylates. Phosphorylated at Ser-898 by PKB; serum-
induced phosphorylation which targets EPHA2 to the cell leading
edge and stimulates cell migration. Phosphorylation by PKB is
inhibited by EFNA1-activated EPHA2 which regulates PKB activity
via a reciprocal regulatory loop. Phosphorylated on tyrosine upon
binding and activation by EFNA1. Phosphorylated residues Tyr-589
and Tyr-595 are required for binding VAV2 and VAV3 while
phosphorylated residues Tyr-736 and Tyr-931 are required for
binding PI3-kinase p85 subunit (PIK3R1, PIK3R2 or PIK3R3). These
phosphorylated residues are critical for recruitment of VAV2 and
VAV3 and PI3-kinase p85 subunit which transduce downstream
signaling to activate RAC1 GTPase and cell migration.
Dephosphorylation of Tyr-931 by PTPRF prevents the interaction of
EPHA2 with NCK1. Phosphorylated at Ser-898 in response to TNF by
RPS6KA1 and RPS6KA3; RPS6KA-EPHA2 signaling pathway controls cell
migration. Phosphorylated at Ser-898 by PKA; blocks cell
retraction induced by EPHA2 kinase activity. Dephosphorylated by
ACP1. {ECO:0000250|UniProtKB:P29317, ECO:0000269|PubMed:18387945}.
-!- PTM: Ubiquitinated by CHIP/STUB1. Ubiquitination is regulated by
the HSP90 chaperone and regulates the receptor stability and
activity through proteasomal degradation. ANKS1A prevents
ubiquitination and degradation. {ECO:0000269|PubMed:20100865}.
-!- DISRUPTION PHENOTYPE: Mice are viable, fertile but exhibit
aberrant development of tail vertebra and susceptibility to
carcinogenesis. {ECO:0000269|PubMed:11287184,
ECO:0000269|PubMed:15054110, ECO:0000269|PubMed:16849550}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X78339; CAA55135.1; -; mRNA.
EMBL; U07634; AAA82113.1; -; mRNA.
EMBL; AK137704; BAE23470.1; -; mRNA.
EMBL; AK144202; BAE25765.1; -; mRNA.
EMBL; AL607087; CAM17000.1; -; Genomic_DNA.
EMBL; AL670285; CAM17000.1; JOINED; Genomic_DNA.
EMBL; AL670285; CAM20402.1; -; Genomic_DNA.
EMBL; AL607087; CAM20402.1; JOINED; Genomic_DNA.
EMBL; CH466615; EDL13361.1; -; Genomic_DNA.
EMBL; BC140960; AAI40961.1; -; mRNA.
EMBL; X76010; CAA53597.1; -; mRNA.
EMBL; X57243; CAA40519.1; -; mRNA.
CCDS; CCDS18869.1; -.
PIR; I48759; I48759.
PIR; I48974; I48974.
PIR; S49004; S49004.
RefSeq; NP_034269.2; NM_010139.3.
UniGene; Mm.2581; -.
ProteinModelPortal; Q03145; -.
SMR; Q03145; -.
BioGrid; 199469; 3.
CORUM; Q03145; -.
DIP; DIP-829N; -.
IntAct; Q03145; 4.
MINT; MINT-3388286; -.
STRING; 10090.ENSMUSP00000006614; -.
GuidetoPHARMACOLOGY; 1822; -.
iPTMnet; Q03145; -.
PhosphoSitePlus; Q03145; -.
EPD; Q03145; -.
MaxQB; Q03145; -.
PaxDb; Q03145; -.
PeptideAtlas; Q03145; -.
PRIDE; Q03145; -.
Ensembl; ENSMUST00000006614; ENSMUSP00000006614; ENSMUSG00000006445.
GeneID; 13836; -.
KEGG; mmu:13836; -.
UCSC; uc008voc.2; mouse.
CTD; 1969; -.
MGI; MGI:95278; Epha2.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; Q03145; -.
KO; K05103; -.
OMA; CSPGFFK; -.
OrthoDB; EOG091G00W0; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-2682334; EPH-Ephrin signaling.
Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
PRO; PR:Q03145; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000006445; -.
CleanEx; MM_EPHA2; -.
Genevisible; Q03145; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0031256; C:leading edge membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
GO; GO:0048320; P:axial mesoderm formation; IMP:MGI.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IMP:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0046849; P:bone remodeling; IMP:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:UniProtKB.
GO; GO:0046058; P:cAMP metabolic process; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0048870; P:cell motility; ISS:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
GO; GO:0030216; P:keratinocyte differentiation; ISO:MGI.
GO; GO:0070309; P:lens fiber cell morphogenesis; IDA:UniProtKB.
GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:MGI.
GO; GO:0032682; P:negative regulation of chemokine production; IMP:MGI.
GO; GO:0001818; P:negative regulation of cytokine production; IMP:MGI.
GO; GO:1901491; P:negative regulation of lymphangiogenesis; IMP:MGI.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0021915; P:neural tube development; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IDA:MGI.
GO; GO:0060035; P:notochord cell development; IMP:MGI.
GO; GO:0014028; P:notochord formation; IMP:MGI.
GO; GO:0048570; P:notochord morphogenesis; IMP:MGI.
GO; GO:0001649; P:osteoblast differentiation; IMP:UniProtKB.
GO; GO:0030316; P:osteoclast differentiation; IDA:UniProtKB.
GO; GO:1904238; P:pericyte cell differentiation; IMP:MGI.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IDA:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0010591; P:regulation of lamellipodium assembly; ISS:UniProtKB.
GO; GO:0070848; P:response to growth factor; ISS:UniProtKB.
GO; GO:0001501; P:skeletal system development; IMP:MGI.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
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; PS01186; EGF_2; 1.
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;
Angiogenesis; Apoptosis; ATP-binding; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome; Differentiation;
Disulfide bond; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 977 Ephrin type-A receptor 2.
/FTId=PRO_0000016801.
TOPO_DOM 26 538 Extracellular. {ECO:0000255}.
TRANSMEM 539 559 Helical. {ECO:0000255}.
TOPO_DOM 560 977 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 205 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 329 433 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 439 530 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 614 876 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 905 969 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 620 628 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 205 Mediates interaction with CLDN4.
{ECO:0000250}.
REGION 607 907 Mediates interaction with ARHGEF16.
{ECO:0000250}.
REGION 887 977 Negatively regulates interaction with
ARHGEF16. {ECO:0000250}.
MOTIF 975 977 PDZ-binding. {ECO:0000255}.
COMPBIAS 187 326 Cys-rich.
ACT_SITE 740 740 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 647 647 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 589 589 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 595 595 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:19131326,
ECO:0000269|PubMed:18387945}.
MOD_RES 629 629 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 648 648 Phosphothreonine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 736 736 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:18387945}.
MOD_RES 773 773 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:19131326,
ECO:0000269|PubMed:18387945}.
MOD_RES 870 870 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 893 893 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 902 902 Phosphoserine.
{ECO:0000250|UniProtKB:P29317}.
MOD_RES 922 922 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 931 931 Phosphotyrosine.
{ECO:0000250|UniProtKB:P29317}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CARBOHYD 436 436 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
DISULFID 69 187 {ECO:0000250}.
DISULFID 104 114 {ECO:0000250}.
MUTAGEN 589 589 Y->E: No significant effect on kinase
activity and loss of binding to VAV2 and
VAV3. Inhibits EFNA1-induced vascular
assembly and RAC1 activation in
endothelial cells, no significant effect
on kinase activity, significant reduction
in phosphorylation and binding to VAV3;
when associated with E-595.
{ECO:0000269|PubMed:16782872,
ECO:0000269|PubMed:18387945}.
MUTAGEN 589 589 Y->F: Inhibits EFNA1-induced vascular
assembly and kinase activity.
{ECO:0000269|PubMed:16782872,
ECO:0000269|PubMed:18387945}.
MUTAGEN 595 595 Y->E: No significant effect on kinase
activity and loss of binding to VAV2 and
VAV3. Inhibits EFNA1-induced vascular
assembly and RAC1 activation in
endothelial cells, no significant effect
on kinase activity, significant reduction
in phosphorylation and binding to VAV3;
when associated with E-589.
{ECO:0000269|PubMed:16782872,
ECO:0000269|PubMed:18387945}.
MUTAGEN 595 595 Y->F: Inhibits EFNA1-induced vascular
assembly and abolishes kinase activity.
{ECO:0000269|PubMed:16782872,
ECO:0000269|PubMed:18387945}.
MUTAGEN 736 736 Y->F: Inhibits EFNA1-induced vascular
assembly and RAC1 activation in
endothelial cells. No significant effect
on kinase activity. Loss of binding to
PI3-kinase p85 subunit.
{ECO:0000269|PubMed:18387945}.
MUTAGEN 740 740 D->N: Loss of kinase activity and binding
to VAV3. {ECO:0000269|PubMed:16782872}.
MUTAGEN 773 773 Y->F: No significant effect on kinase
activity. Significant reduction in
phosphorylation.
{ECO:0000269|PubMed:18387945}.
MUTAGEN 931 931 Y->F: Inhibits EFNA1-induced vascular
assembly and RAC1 activation in
endothelial cells. Inhibits kinase
activity. Loss of binding to VAV3 and
PI3-kinase p85 subunit.
{ECO:0000269|PubMed:18387945}.
CONFLICT 5 5 A -> T (in Ref. 1; CAA55135).
{ECO:0000305}.
CONFLICT 112 113 SS -> HA (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 189 189 A -> R (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 209 209 R -> C (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 244 244 P -> A (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 258 260 IGQ -> SE (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 291 291 C -> S (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 339 340 IG -> C (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 371 372 WP -> CA (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 383 383 S -> T (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 457 457 W -> R (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 485 485 V -> G (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 511 511 L -> W (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 534 534 A -> R (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 678 678 R -> P (in Ref. 1; CAA55135).
{ECO:0000305}.
CONFLICT 681 681 G -> A (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 819 820 YW -> LL (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 878 878 A -> R (in Ref. 2; AAA82113).
{ECO:0000305}.
CONFLICT 919 920 MQ -> IE (in Ref. 2; AAA82113).
{ECO:0000305}.
SEQUENCE 977 AA; 108852 MW; 66338CE7EF2DEE02 CRC64;
MELRAVGFCL ALLWGCALAA AAAQGKEVVL LDFAAMKGEL GWLTHPYGKG WDLMQNIMDD
MPIYMYSVCN VVSGDQDNWL RTNWVYREEA ERIFIELKFT VRDCNSFPGG ASSCKETFNL
YYAESDVDYG TNFQKRQFTK IDTIAPDEIT VSSDFEARNV KLNVEERMVG PLTRKGFYLA
FQDIGACVAL LSVRVYYKKC PEMLQSLARF PETIAVAVSD TQPLATVAGT CVDHAVVPYG
GEGPLMHCTV DGEWLVPIGQ CLCQEGYEKV EDACRACSPG FFKSEASESP CLECPEHTLP
STEGATSCQC EEGYFRAPED PLSMSCTRPP SAPNYLTAIG MGAKVELRWT APKDTGGRQD
IVYSVTCEQC WPESGECGPC EASVRYSEPP HALTRTSVTV SDLEPHMNYT FAVEARNGVS
GLVTSRSFRT ASVSINQTEP PKVRLEDRST TSLSVTWSIP VSQQSRVWKY EVTYRKKGDA
NSYNVRRTEG FSVTLDDLAP DTTYLVQVQA LTQEGQGAGS KVHEFQTLST EGSANMAVIG
GVAVGVVLLL VLAGVGLFIH RRRRNLRARQ SSEDVRFSKS EQLKPLKTYV DPHTYEDPNQ
AVLKFTTEIH PSCVARQKVI GAGEFGEVYK GTLKASSGKK EIPVAIKTLK AGYTEKQRVD
FLSEASIMGQ FSHHNIIRLE GVVSKYKPMM IITEYMENGA LDKFLREKDG EFSVLQLVGM
LRGIASGMKY LANMNYVHRD LAARNILVNS NLVCKVSDFG LSRVLEDDPE ATYTTSGGKI
PIRWTAPEAI SYRKFTSASD VWSYGIVMWE VMTYGERPYW ELSNHEVMKA INDGFRLPTP
MDCPSAIYQL MMQCWQQERS RRPKFADIVS ILDKLIRAPD SLKTLADFDP RVSIRLPSTS
GSEGVPFRTV SEWLESIKMQ QYTEHFMVAG YTAIEKVVQM SNEDIKRIGV RLPGHQKRIA
YSLLGLKDQV NTVGIPI


Related products :

Catalog number Product name Quantity
EIAAB13074 Eck,Epha2,Ephrin type-A receptor 2,Epithelial cell kinase,Mouse,Mus musculus,Myk2,Sek2,Tyrosine-protein kinase receptor ECK,Tyrosine-protein kinase receptor MPK-5,Tyrosine-protein kinase receptor SEK-
EIAAB13105 Ephb2,Ephrin type-B receptor 2,Epth3,Mouse,Mus musculus,Neural kinase,Nuk,Nuk receptor tyrosine kinase,Sek3,Tyrosine-protein kinase receptor EPH-3,Tyrosine-protein kinase receptor SEK-3
EIAAB13072 EPH,EPH tyrosine kinase,EPH tyrosine kinase 1,EPHA1,Ephrin type-A receptor 1,EPHT,EPHT1,Erythropoietin-producing hepatoma receptor,hEpha1,Homo sapiens,Human,Tyrosine-protein kinase receptor EPH
E0039h ELISA kit CD135,Fetal liver kinase-2,FL cytokine receptor,FLK2,FLK-2,FLT3,FLT-3,Fms-like tyrosine kinase 3,Homo sapiens,Human,Receptor-type tyrosine-protein kinase FLT3,Stem cell tyrosine kinase 1,ST 96T
U0039h CLIA CD135,Fetal liver kinase-2,FL cytokine receptor,FLK2,FLK-2,FLT3,FLT-3,Fms-like tyrosine kinase 3,Homo sapiens,Human,Receptor-type tyrosine-protein kinase FLT3,Stem cell tyrosine kinase 1,STK1,STK 96T
E0039h ELISA CD135,Fetal liver kinase-2,FL cytokine receptor,FLK2,FLK-2,FLT3,FLT-3,Fms-like tyrosine kinase 3,Homo sapiens,Human,Receptor-type tyrosine-protein kinase FLT3,Stem cell tyrosine kinase 1,STK1,ST 96T
EIAAB13077 EK4,EPHA3,EPH-like kinase 4,Eph-like tyrosine kinase 1,Ephrin type-A receptor 3,ETK,ETK1,HEK,HEK,hEK4,Homo sapiens,Human,Human embryo kinase,TYRO4,Tyrosine-protein kinase receptor ETK1,Tyrosine-protei
EIAAB13075 ECK,EPHA2,Ephrin type-A receptor 2,Epithelial cell kinase,Homo sapiens,Human,Tyrosine-protein kinase receptor ECK
EIAAB13100 EK6,ELK,ELK,EPH tyrosine kinase 2,EPHB1,EPH-like kinase 6,Ephrin type-B receptor 1,EPHT2,hEK6,HEK6,Homo sapiens,Human,NET,NET,Neuronally-expressed EPH-related tyrosine kinase,Tyrosine-protein kinase r
EIAAB33008 CCK4,CCK-4,Colon carcinoma kinase 4,Homo sapiens,Human,Inactive tyrosine-protein kinase 7,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,PTK7,Tyrosine-protein kinase-like 7
U0039m CLIA Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase receptor fl 96T
E0039m ELISA Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase receptor f 96T
EIAAB42378 Angiopoietin-1 receptor,Homo sapiens,hTIE2,Human,p140 TEK,TEK,TIE2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
EIAAB42377 Angiopoietin-1 receptor,HYK,Hyk,Mouse,mTIE2,Mus musculus,p140 TEK,STK1,Tek,Tie2,Tie-2,Tunica interna endothelial cell kinase,Tyrosine-protein kinase receptor TEK,Tyrosine-protein kinase receptor TIE-2
EIAAB13081 Epha4,Ephrin type-A receptor 4,Mouse,Mus musculus,Sek,Sek1,Tyrosine-protein kinase receptor MPK-3,Tyrosine-protein kinase receptor SEK-1
E0039m ELISA kit Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase recep 96T
EIAAB33010 Inactive tyrosine-protein kinase 7,Mouse,Mus musculus,Protein chuzhoi,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,Ptk7,Tyrosine-protein kinase-like 7
E0147m ELISA kit Embryonic receptor kinase 2,Emrk2,Flt,Flt1,FLT-1,Fms-like tyrosine kinase 1,Mouse,Mus musculus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
U0147m CLIA Embryonic receptor kinase 2,Emrk2,Flt,Flt1,FLT-1,Fms-like tyrosine kinase 1,Mouse,Mus musculus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
E0147m ELISA Embryonic receptor kinase 2,Emrk2,Flt,Flt1,FLT-1,Fms-like tyrosine kinase 1,Mouse,Mus musculus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
U0147h CLIA FLT,FLT1,FLT-1,Fms-like tyrosine kinase 1,FRT,Homo sapiens,Human,Tyrosine-protein kinase FRT,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,Vascular permeabili 96T
E0147h ELISA FLT,FLT1,FLT-1,Fms-like tyrosine kinase 1,FRT,Homo sapiens,Human,Tyrosine-protein kinase FRT,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,Vascular permeabil 96T
E0147h ELISA kit FLT,FLT1,FLT-1,Fms-like tyrosine kinase 1,FRT,Homo sapiens,Human,Tyrosine-protein kinase FRT,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,Vascular perm 96T
EIAAB13073 Embryonic stem cell kinase,Epha1,Ephrin type-A receptor 1,Esk,mEpha1,Mouse,Mus musculus,Tyrosine-protein kinase receptor ESK
EIAAB13080 EK8,EPHA4,EPH-like kinase 8,Ephrin type-A receptor 4,hEK8,HEK8,Homo sapiens,Human,SEK,TYRO1,Tyrosine-protein kinase receptor SEK,Tyrosine-protein kinase TYRO1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur