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Ephrin type-A receptor 1 (mEpha1) (EC 2.7.10.1) (Embryonic stem cell kinase) (Tyrosine-protein kinase receptor ESK)

 EPHA1_MOUSE             Reviewed;         977 AA.
Q60750; Q8CED9; Q9ESJ2;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
22-NOV-2017, entry version 170.
RecName: Full=Ephrin type-A receptor 1;
Short=mEpha1;
EC=2.7.10.1;
AltName: Full=Embryonic stem cell kinase;
AltName: Full=Tyrosine-protein kinase receptor ESK;
Flags: Precursor;
Name=Epha1; Synonyms=Esk;
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], TISSUE SPECIFICITY, AND EFNA1
LIGAND-BINDING.
PubMed=11519828; DOI=10.3109/08977190109029118;
Coulthard M.G., Lickliter J.D., Subanesan N., Chen K., Webb G.C.,
Lowry A.J., Koblar S., Bottema C.D., Boyd A.W.;
"Characterization of the Epha1 receptor tyrosine kinase: expression in
epithelial tissues.";
Growth Factors 18:303-317(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Skin;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 281-814.
STRAIN=129/Sv;
PubMed=8552593; DOI=10.1073/pnas.93.1.145;
Lickliter J.D., Smith F.M., Olsson J.E., Mackwell K.L., Boyd A.W.;
"Embryonic stem cells express multiple Eph-subfamily receptor tyrosine
kinases.";
Proc. Natl. Acad. Sci. U.S.A. 93:145-150(1996).
[4]
DISRUPTION PHENOTYPE, FUNCTION IN APOPTOSIS, AND TISSUE SPECIFICITY.
PubMed=18802966; DOI=10.1002/dvg.20434;
Duffy S.L., Coulthard M.G., Spanevello M.D., Herath N.I., Yeadon T.M.,
McCarron J.K., Carter J.C., Tonks I.D., Kay G.F., Phillips G.E.,
Boyd A.W.;
"Generation and characterization of EphA1 receptor tyrosine kinase
reporter knockout mice.";
Genesis 46:553-561(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[6]
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).
[7]
STRUCTURE BY NMR OF 446-539.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the second fibronectin type III domain of
mouse ephrin type-A receptor 1.";
Submitted (NOV-2005) to the PDB data bank.
-!- 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. Binds with a low affinity EFNA3 and EFNA4 and with a
high affinity to EFNA1 which most probably constitutes its
cognate/functional ligand. Upon activation by EFNA1 induces cell
attachment to the extracellular matrix inhibiting cell spreading
and motility through regulation of ILK and downstream RHOA and
RAC. Plays also a role in angiogenesis and regulates cell
proliferation. May play a role in apoptosis.
{ECO:0000269|PubMed:18802966}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2
and PI3-kinase upon activation by EFNA1; regulates T-lymphocytes
migration. Interacts (via SAM domain) with ILK (via ANK repeats);
stimulated by EFNA1 but independent of the kinase activity of
EPHA1. Interacts (kinase activity-dependent) with PTK2/FAK1 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Preferentially expressed in epithelial cells
including skin, kidney, liver and thymus (PubMed:11519828,
PubMed:18802966). Expressed in myogenic progenitor cells
(PubMed:27446912). {ECO:0000269|PubMed:11519828,
ECO:0000269|PubMed:18802966, ECO:0000269|PubMed:27446912}.
-!- DEVELOPMENTAL STAGE: In myogenic progenitor cells, expressed
during the acquisition of muscle stem cell properties, from E18.5
to adulthood. {ECO:0000269|PubMed:27446912}.
-!- PTM: Phosphorylated. Autophosphorylation is stimulated by its
ligand EFNA1 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice display a partially-penetrant
uterovaginal and tail development defects. The uterovaginal defect
is due to a defect in apoptosis during development.
{ECO:0000269|PubMed:18802966}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AF131197; AAG12206.1; -; mRNA.
EMBL; AK028478; BAC25971.1; -; mRNA.
EMBL; U18084; AAC52384.1; -; mRNA.
CCDS; CCDS20067.1; -.
RefSeq; NP_076069.2; NM_023580.4.
UniGene; Mm.133330; -.
PDB; 1X5A; NMR; -; A=446-539.
PDBsum; 1X5A; -.
ProteinModelPortal; Q60750; -.
SMR; Q60750; -.
BioGrid; 199468; 1.
IntAct; Q60750; 4.
MINT; MINT-7013408; -.
STRING; 10090.ENSMUSP00000073099; -.
iPTMnet; Q60750; -.
PhosphoSitePlus; Q60750; -.
MaxQB; Q60750; -.
PaxDb; Q60750; -.
PeptideAtlas; Q60750; -.
PRIDE; Q60750; -.
Ensembl; ENSMUST00000073387; ENSMUSP00000073099; ENSMUSG00000029859.
GeneID; 13835; -.
KEGG; mmu:13835; -.
UCSC; uc009brc.1; mouse.
CTD; 2041; -.
MGI; MGI:107381; Epha1.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOGENOM; HOG000233856; -.
HOVERGEN; HBG062180; -.
InParanoid; Q60750; -.
KO; K05102; -.
OMA; QAYEDPA; -.
OrthoDB; EOG091G00W0; -.
PhylomeDB; Q60750; -.
TreeFam; TF315363; -.
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.
EvolutionaryTrace; Q60750; -.
PRO; PR:Q60750; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000029859; -.
CleanEx; MM_EPHA1; -.
ExpressionAtlas; Q60750; baseline and differential.
Genevisible; Q60750; MM.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
CDD; cd10479; EphR_LBD_A1; 1.
CDD; cd00063; FN3; 2.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034251; EphA1_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; 1.
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;
3D-structure; Angiogenesis; ATP-binding; Cell adhesion; Cell membrane;
Complete proteome; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 977 Ephrin type-A receptor 1. {ECO:0000250}.
/FTId=PRO_0000016799.
TOPO_DOM 27 548 Extracellular. {ECO:0000255}.
TRANSMEM 549 569 Helical. {ECO:0000255}.
TOPO_DOM 570 977 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 210 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 333 446 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 448 539 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 625 885 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 914 977 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 631 639 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 975 977 PDZ-binding. {ECO:0000255}.
COMPBIAS 192 330 Cys-rich.
ACT_SITE 750 750 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 657 657 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 600 600 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 606 606 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 782 782 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 907 907 Phosphoserine.
{ECO:0000250|UniProtKB:P21709}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000250|UniProtKB:P21709}.
CARBOHYD 415 415 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 479 479 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 163 163 G -> D (in Ref. 1; AAG12206).
{ECO:0000305}.
CONFLICT 422 422 S -> P (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 504 504 L -> R (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 521 521 T -> A (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 590 590 D -> G (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 636 636 F -> Y (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 660 660 K -> R (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 720 720 D -> G (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 769 769 F -> L (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 797 797 E -> G (in Ref. 3; AAC52384).
{ECO:0000305}.
CONFLICT 817 817 M -> T (in Ref. 1; AAG12206).
{ECO:0000305}.
STRAND 456 460 {ECO:0000244|PDB:1X5A}.
STRAND 463 467 {ECO:0000244|PDB:1X5A}.
STRAND 481 487 {ECO:0000244|PDB:1X5A}.
STRAND 492 506 {ECO:0000244|PDB:1X5A}.
STRAND 512 520 {ECO:0000244|PDB:1X5A}.
STRAND 522 524 {ECO:0000244|PDB:1X5A}.
STRAND 532 535 {ECO:0000244|PDB:1X5A}.
SEQUENCE 977 AA; 108578 MW; AB78D6E6C8B2E7F4 CRC64;
MERRWPLGLA LLLLLLCAPL PPGARAEEVT LMDTSTAQGE LGWLLDPPET GWSEVQQMLN
GTPLYMYQDC PIQEGGDTDH WLRSNWIYRG EEASRIYVEL QFTVRDCKSF PGGAGPLGCK
ETFNLFYMES DQDVGIQLRR PLFQKVTTVA ADQSFTIRDL ASGSVKLNVE RCSLGHLTRR
GLYLAFHNPG SCVALVSVRV FYQRCAETVH GLAHFPDTLP GPGGLVEVAG TCLSHAQISL
GSSGTPRMHC SPDGEWLVPV GQCQCEPGYE ESSGNVGCTA CPTGFYRVDM NTLRCLKCPQ
HSIAESEGST ICTCENGHYR APGEGPQVAC TRPPSAPQNL SFSTSGTQLS LRWEPPRDTG
GRHDIRYSVE CLQCRGIAQD GGPCQPCGKG VHFSPAASGL TTSTVQVQGL EPYANYTFTV
KSQNRVSGLD SSSPSSASLS INMGHAESLS GLSLKLVKKE PRQLELTWAG SRPRNPGGNL
SYELHVLNQD EEWHQMVLEP RVLLTKLQPD TTYIVRVRTL TPLGPGPFSP DHEFRTSPPV
SRSLTGGEIV AVIFGLLLGI ALLIGIYVFR SRRGQRQRQQ RQRERTTNVD REDKLWLKPY
VDLQAYEDPA QGALDFAQEL DPAWLIVDTV IGEGEFGEVY RGALRLPSQD CKTVAIKTLK
DTSPDGYWWN FLREATIMGQ FNHPHILRLE GVITKRKPIM IITEFMENGA LDAFLKERED
QLAPGQLVAM LLGIASGMNC LSGHNYVHRD LAARNILVNQ NLCCKVSDFG LTRLLDDFDG
TYETQGGKIP IRWTAPEAIA HRIFTTASDV WSFGIVMWEV LSFGDKPYGE MSNQEVMKSI
EDGYRLPPPV DCPAPLYELM KNCWAYDRAR RPHFLQLQAH LEQLLTDPHS LRTIANFDPR
VTLRLPSLSG SDGIPYRSVS EWLESIRMKR YILHFRSAGL DTMECVLELT AEDLTQMGIT
LPGHQKRILC SIQGFKD


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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
EIAAB13081 Epha4,Ephrin type-A receptor 4,Mouse,Mus musculus,Sek,Sek1,Tyrosine-protein kinase receptor MPK-3,Tyrosine-protein kinase receptor SEK-1
EIAAB13096 EEK,EK3,EPH- and ELK-related kinase,EPHA8,EPH-like kinase 3,Ephrin type-A receptor 8,hEK3,HEK3,Homo sapiens,Human,KIAA1459,Tyrosine-protein kinase receptor EEK
EIAAB13095 Eek,EPH- and ELK-related kinase,Epha8,Ephrin type-A receptor 8,Mouse,Mus musculus,Tyrosine-protein kinase receptor EEK
EIAAB13094 Eek,EPH- and ELK-related kinase,Epha8,Ephrin type-A receptor 8,Rat,Rattus norvegicus,Tyrosine-protein kinase receptor EEK
EIAAB13108 Developmental kinase 5,Ephb3,Ephrin type-B receptor 3,Etk2,Mdk5,mDK-5,Mouse,Mus musculus,Sek4,Tyrosine-protein kinase receptor SEK-4
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
EIAAB43303 Kinase of embryonic stem cells,Kos1,Mouse,Mus musculus,Non-receptor tyrosine-protein kinase TNK1,Tnk1
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
EIAAB13091 Developmental kinase 1,EBK,Ebk,Ehk3,EHK-3,Embryonic brain kinase,EPH homology kinase 3,Epha7,Ephrin type-A receptor 7,Mdk1,mDK-1,Mouse,Mus musculus


 

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