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Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (HYK) (STK1) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (mTIE2) (p140 TEK) (CD antigen CD202b)

 TIE2_MOUSE              Reviewed;        1122 AA.
Q02858;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
10-FEB-2021, entry version 199.
RecName: Full=Angiopoietin-1 receptor;
EC=2.7.10.1;
AltName: Full=Endothelial tyrosine kinase;
AltName: Full=HYK;
AltName: Full=STK1;
AltName: Full=Tunica interna endothelial cell kinase;
AltName: Full=Tyrosine kinase with Ig and EGF homology domains-2;
AltName: Full=Tyrosine-protein kinase receptor TEK;
AltName: Full=Tyrosine-protein kinase receptor TIE-2;
Short=mTIE2;
AltName: Full=p140 TEK;
AltName: CD_antigen=CD202b;
Flags: Precursor;
Name=Tek; Synonyms=Hyk, Tie-2, Tie2;
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].
STRAIN=BALB/cJ; TISSUE=Lung;
PubMed=8415706; DOI=10.1073/pnas.90.20.9355;
Sato T.N., Qin Y., Kozak C.A., Andus K.L.;
"Tie-1 and tie-2 define another class of putative receptor tyrosine kinase
genes expressed in early embryonic vascular system.";
Proc. Natl. Acad. Sci. U.S.A. 90:9355-9358(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CD-1; TISSUE=Embryonic heart;
PubMed=8386827;
Dumont D.J., Gradwol G.J., Fong G.-H., Auerbach R., Breitman M.L.;
"The endothelial-specific receptor tyrosine kinase, tek, is a member of a
new subfamily of receptors.";
Oncogene 8:1293-1301(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryonic stem cell;
PubMed=1282811; DOI=10.1016/0006-291x(92)90280-x;
Horita K., Yagi T., Kohmura N., Tomooka Y., Ikawa Y., Aizawa S.;
"A novel tyrosine kinase, hyk, expressed in murine embryonic stem cells.";
Biochem. Biophys. Res. Commun. 189:1747-1753(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=8217221;
Runting A.S., Stacker S.A., Wilks A.F.;
"Tie2, a putative protein tyrosine kinase from a new class of cell surface
receptor.";
Growth Factors 9:99-105(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8187650;
Schnuerch H., Risau W.;
"Expression of tie-2, a member of a novel family of receptor tyrosine
kinases, in the endothelial cell lineage.";
Development 119:957-968(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Hematopoietic stem cell;
PubMed=8395828; DOI=10.1006/bbrc.1993.2045;
Iwama A., Hamaguchi I., Hashiyama M., Murayama Y., Yasunaga K., Suda T.;
"Molecular cloning and characterization of mouse TIE and TEK receptor
tyrosine kinase genes and their expression in hematopoietic stem cells.";
Biochem. Biophys. Res. Commun. 195:301-309(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 822-1122.
STRAIN=CD-1; TISSUE=Embryonic heart;
PubMed=1630810;
Dumont D.J., Yamaguchi T.P., Conlon R.A., Rossant J., Breitman M.L.;
"Tek, a novel tyrosine kinase gene located on mouse chromosome 4, is
expressed in endothelial cells and their presumptive precursors.";
Oncogene 7:1471-1480(1992).
[8]
DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-853, CATALYTIC ACTIVITY, AND
FUNCTION.
PubMed=7958865; DOI=10.1101/gad.8.16.1897;
Dumont D.J., Gradwohl G., Fong G.H., Puri M.C., Gertsenstein M.,
Auerbach A., Breitman M.L.;
"Dominant-negative and targeted null mutations in the endothelial receptor
tyrosine kinase, tek, reveal a critical role in vasculogenesis of the
embryo.";
Genes Dev. 8:1897-1909(1994).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=7596437; DOI=10.1038/376070a0;
Sato T.N., Tozawa Y., Deutsch U., Wolburg-Buchholz K., Fujiwara Y.,
Gendron-Maguire M., Gridley T., Wolburg H., Risau W., Qin Y.;
"Distinct roles of the receptor tyrosine kinases Tie-1 and Tie-2 in blood
vessel formation.";
Nature 376:70-74(1995).
[10]
INTERACTION WITH PIK3R1, MUTAGENESIS OF TYR-1100, AND FUNCTION IN
ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE AND AKT1.
PubMed=9632797; DOI=10.1128/mcb.18.7.4131;
Kontos C.D., Stauffer T.P., Yang W.P., York J.D., Huang L., Blanar M.A.,
Meyer T., Peters K.G.;
"Tyrosine 1101 of Tie2 is the major site of association of p85 and is
required for activation of phosphatidylinositol 3-kinase and Akt.";
Mol. Cell. Biol. 18:4131-4140(1998).
[11]
INTERACTION WITH GRB2; GRB7, GRB14, PTPN11/SHP2 AND PIK3R1, FUNCTION IN
PHOSPHORYLATION OF GRB7 AND PIK3R1, AND MUTAGENESIS OF TYR-1100.
PubMed=10521483; DOI=10.1074/jbc.274.43.30896;
Jones N., Master Z., Jones J., Bouchard D., Gunji Y., Sasaki H., Daly R.,
Alitalo K., Dumont D.J.;
"Identification of Tek/Tie2 binding partners. Binding to a multifunctional
docking site mediates cell survival and migration.";
J. Biol. Chem. 274:30896-30905(1999).
[12]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPRB.
PubMed=10557082; DOI=10.1038/sj.onc.1202992;
Fachinger G., Deutsch U., Risau W.;
"Functional interaction of vascular endothelial-protein-tyrosine
phosphatase with the angiopoietin receptor Tie-2.";
Oncogene 18:5948-5953(1999).
[13]
ANTI-APOPTOTIC FUNCTION.
PubMed=11375937; DOI=10.1093/embo-reports/kve093;
Jones N., Voskas D., Master Z., Sarao R., Jones J., Dumont D.J.;
"Rescue of the early vascular defects in Tek/Tie2 null mice reveals an
essential survival function.";
EMBO Rep. 2:438-445(2001).
[14]
INTERACTION WITH ANGPT1 AND ANGPT2, AND DOMAIN.
PubMed=12427764; DOI=10.1074/jbc.m208550200;
Fiedler U., Krissl T., Koidl S., Weiss C., Koblizek T., Deutsch U.,
Martiny-Baron G., Marme D., Augustin H.G.;
"Angiopoietin-1 and angiopoietin-2 share the same binding domains in the
Tie-2 receptor involving the first Ig-like loop and the epidermal growth
factor-like repeats.";
J. Biol. Chem. 278:1721-1727(2003).
[15]
PHOSPHORYLATION AT TYR-1100 AND TYR-1106, MUTAGENESIS OF LYS-853; TYR-1100
AND TYR-1106, FUNCTION IN DOK2 PHOSPHORYLATION, AND INTERACTION WITH DOK2.
PubMed=12665569; DOI=10.1128/mcb.23.8.2658-2668.2003;
Jones N., Chen S.H., Sturk C., Master Z., Tran J., Kerbel R.S.,
Dumont D.J.;
"A unique autophosphorylation site on Tie2/Tek mediates Dok-R
phosphotyrosine binding domain binding and function.";
Mol. Cell. Biol. 23:2658-2668(2003).
[16]
FUNCTION AS ANGPT4 RECEPTOR AND IN ACTIVATION OF AKT1, INTERACTION WITH
ANGPT4, AND AUTOPHOSPHORYLATION.
PubMed=15284220; DOI=10.1096/fj.03-1466com;
Lee H.J., Cho C.H., Hwang S.J., Choi H.H., Kim K.T., Ahn S.Y., Kim J.H.,
Oh J.L., Lee G.M., Koh G.Y.;
"Biological characterization of angiopoietin-3 and angiopoietin-4.";
FASEB J. 18:1200-1208(2004).
[17]
INTERACTION WITH PTPRB.
PubMed=19451274; DOI=10.1083/jcb.200811159;
Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F.,
Deutsch U., Nottebaum A.F., Vestweber D.;
"VE-PTP controls blood vessel development by balancing Tie-2 activity.";
J. Cell Biol. 185:657-671(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Spleen;
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).
[19]
INTERACTION WITH GRB14, AND FUNCTION IN GRB14 PHOSPHORYLATION.
PubMed=20973951; DOI=10.1186/1478-811x-8-30;
Sturk C., Dumont D.J.;
"Tyrosine phosphorylation of Grb14 by Tie2.";
Cell Commun. Signal. 8:30-30(2010).
[20]
DISRUPTION PHENOTYPE.
PubMed=27270174; DOI=10.1172/jci85830;
Souma T., Tompson S.W., Thomson B.R., Siggs O.M., Kizhatil K.,
Yamaguchi S., Feng L., Limviphuvadh V., Whisenhunt K.N., Maurer-Stroh S.,
Yanovitch T.L., Kalaydjieva L., Azmanov D.N., Finzi S., Mauri L.,
Javadiyan S., Souzeau E., Zhou T., Hewitt A.W., Kloss B., Burdon K.P.,
Mackey D.A., Allen K.F., Ruddle J.B., Lim S.H., Rozen S., Tran-Viet K.N.,
Liu X., John S., Wiggs J.L., Pasutto F., Craig J.E., Jin J., Quaggin S.E.,
Young T.L.;
"Angiopoietin receptor TEK mutations underlie primary congenital glaucoma
with variable expressivity.";
J. Clin. Invest. 126:2575-2587(2016).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial
cell survival, proliferation, migration, adhesion and cell spreading,
reorganization of the actin cytoskeleton, but also maintenance of
vascular quiescence. Has anti-inflammatory effects by preventing the
leakage of proinflammatory plasma proteins and leukocytes from blood
vessels. Required for normal angiogenesis and heart development during
embryogenesis. Required for post-natal hematopoiesis. After birth,
activates or inhibits angiogenesis, depending on the context. Inhibits
angiogenesis and promotes vascular stability in quiescent vessels,
where endothelial cells have tight contacts. In quiescent vessels,
ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes
with TEK molecules from adjoining cells, and this leads to preferential
activation of phosphatidylinositol 3-kinase and the AKT1 signaling
cascades. In migrating endothelial cells that lack cell-cell adhesions,
ANGT1 recruits TEK to contacts with the extracellular matrix, leading
to the formation of focal adhesion complexes, activation of PTK2/FAK
and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately
to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers
receptor dimerization and autophosphorylation at specific tyrosine
residues that then serve as binding sites for scaffold proteins and
effectors. Signaling is modulated by ANGPT2 that has lower affinity for
TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but
inhibits ANGPT1-mediated signaling by competing for the same binding
site. Signaling is also modulated by formation of heterodimers with
TIE1, and by proteolytic processing that gives rise to a soluble TEK
extracellular domain. The soluble extracellular domain modulates
signaling by functioning as decoy receptor for angiopoietins. TEK
phosphorylates DOK2, GRB7, GRB14, PIK3R1, SHC1 and TIE1.
{ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:12665569,
ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:20973951,
ECO:0000269|PubMed:7596437, ECO:0000269|PubMed:7958865,
ECO:0000269|PubMed:9632797}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
ECO:0000269|PubMed:7958865};
-!- ACTIVITY REGULATION: Angiopoietin binding leads to receptor
dimerization and activation by autophosphorylation at Tyr-990 on the
kinase activation loop. {ECO:0000250}.
-!- SUBUNIT: Homodimer. Heterodimer with TIE1. Interacts with ANGPT1,
ANGPT2 and ANGPT4. At cell-cell contacts in quiescent cells, forms a
signaling complex composed of ANGPT1 plus TEK molecules from two
adjoining cells. In the absence of endothelial cell-cell contacts,
interaction with ANGPT1 mediates contacts with the extracellular
matrix. Interacts (tyrosine phosphorylated) with TNIP2. Interacts
(tyrosine phosphorylated) with SHC1 (via SH2 domain) (By similarity).
Interacts with PTPRB; this promotes endothelial cell-cell adhesion.
Interacts with DOK2, GRB2, GRB7, GRB14, PIK3R1 and PTPN11/SHP2.
Colocalizes with DOK2 at contacts with the extracellular matrix in
migrating cells. {ECO:0000250, ECO:0000269|PubMed:10521483,
ECO:0000269|PubMed:12427764, ECO:0000269|PubMed:12665569,
ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:19451274,
ECO:0000269|PubMed:20973951, ECO:0000269|PubMed:9632797}.
-!- INTERACTION:
Q02858; Q60631: Grb2; NbExp=3; IntAct=EBI-7099626, EBI-1688;
Q02858; Q03160: Grb7; NbExp=3; IntAct=EBI-7099626, EBI-7100053;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cell junction {ECO:0000250}. Cell junction, focal adhesion
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Secreted
{ECO:0000250}. Note=Recruited to cell-cell contacts in quiescent
endothelial cells. Colocalizes with the actin cytoskeleton and at actin
stress fibers during cell spreading. Recruited to the lower surface of
migrating cells, especially the rear end of the cell. Proteolytic
processing gives rise to a soluble extracellular domain that is
secreted (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Specifically expressed in developing vascular
endothelial cells. Abundantly expressed in lung and heart, moderately
in brain, liver and kidney, and weakly in thymus, spleen and testis.
{ECO:0000269|PubMed:8395828}.
-!- DEVELOPMENTAL STAGE: Expression detectable in day 8.5 embryos.
-!- DOMAIN: The soluble extracellular domain is functionally active in
angiopoietin binding and can modulate the activity of the membrane-
bound form by competing for angiopoietins. {ECO:0000250}.
-!- PTM: Proteolytic processing leads to the shedding of the extracellular
domain (soluble TIE-2 alias sTIE-2). {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues in response to ligand
binding. Autophosphorylation occurs in trans, i.e. one subunit of the
dimeric receptor phosphorylates tyrosine residues on the other subunit.
Autophosphorylation occurs in a sequential manner, where Tyr-990 in the
kinase activation loop is phosphorylated first, followed by
autophosphorylation at Tyr-1106 and at additional tyrosine residues.
ANGPT1-induced phosphorylation is impaired during hypoxia, due to
increased expression of ANGPT2 (By similarity). Phosphorylation is
important for interaction with GRB14, PIK3R1 and PTPN11.
Phosphorylation at Tyr-1100 is important for interaction with GRB2 and
GRB7. Phosphorylation at Tyr-1106 is important for interaction with
DOK2 and for coupling to downstream signal transduction pathways in
endothelial cells. Dephosphorylated by PTPRB. {ECO:0000250,
ECO:0000269|PubMed:10557082, ECO:0000269|PubMed:12665569}.
-!- PTM: Ubiquitinated. The phosphorylated receptor is ubiquitinated and
internalized, leading to its degradation (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonically lethal. Embryos die at about 10
dpc, due to strongly decreased numbers of blood vessel endothelial
cells, leading to severe hemorrhaging, and due to defects in heart
trabeculae development. Mice display a general malformation of the
vascular network with defective sprouting and dilated blood vessels.
Conditional by inversion allele knockout mice don't have Schlemm's
canal. Haploinsufficient mice developed a severely hypomorphic
Schlemm's canal with convolutions and focal narrowing
(PubMed:27270174). {ECO:0000269|PubMed:27270174,
ECO:0000269|PubMed:7596437, ECO:0000269|PubMed:7958865}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Tie subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
---------------------------------------------------------------------------
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EMBL; X71426; CAA50557.1; -; mRNA.
EMBL; X67553; CAA47857.1; -; mRNA.
EMBL; D13738; BAA02883.1; -; mRNA.
EMBL; S67051; AAB28663.1; -; mRNA.
CCDS; CCDS71421.1; -.
PIR; I54237; I54237.
PIR; JH0771; JH0771.
PIR; JN0712; JN0712.
RefSeq; NP_001277478.1; NM_001290549.1.
SMR; Q02858; -.
BioGRID; 204107; 5.
IntAct; Q02858; 7.
MINT; Q02858; -.
STRING; 10090.ENSMUSP00000099862; -.
BindingDB; Q02858; -.
ChEMBL; CHEMBL5199; -.
DrugCentral; Q02858; -.
GlyConnect; 2128; 1 N-Linked glycan (1 site).
GlyGen; Q02858; 9 sites.
iPTMnet; Q02858; -.
PhosphoSitePlus; Q02858; -.
CPTAC; non-CPTAC-3433; -.
jPOST; Q02858; -.
MaxQB; Q02858; -.
PaxDb; Q02858; -.
PRIDE; Q02858; -.
Antibodypedia; 2050; 1359 antibodies.
Ensembl; ENSMUST00000071168; ENSMUSP00000071162; ENSMUSG00000006386.
GeneID; 21687; -.
KEGG; mmu:21687; -.
UCSC; uc008tsk.2; mouse.
CTD; 7010; -.
MGI; MGI:98664; Tek.
eggNOG; KOG0200; Eukaryota.
GeneTree; ENSGT00940000158840; -.
InParanoid; Q02858; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-210993; Tie2 Signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
BioGRID-ORCS; 21687; 0 hits in 17 CRISPR screens.
PRO; PR:Q02858; -.
Proteomes; UP000000589; Chromosome 4.
RNAct; Q02858; protein.
Bgee; ENSMUSG00000006386; Expressed in brain blood vessel and 297 other tissues.
ExpressionAtlas; Q02858; baseline and differential.
Genevisible; Q02858; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; ISO:MGI.
GO; GO:0034451; C:centriolar satellite; ISO:MGI.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; ISM:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005902; C:microvillus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; IPI:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; TAS:DFLAT.
GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0072012; P:glomerulus vasculature development; ISO:MGI.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0060347; P:heart trabecula formation; IMP:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; ISO:MGI.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:MGI.
GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; IDA:MGI.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISS:UniProtKB.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IGI:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:DFLAT.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; IMP:MGI.
GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
GO; GO:0001936; P:regulation of endothelial cell proliferation; TAS:DFLAT.
GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; ISS:UniProtKB.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IGI:MGI.
GO; GO:0043627; P:response to estrogen; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; ISO:MGI.
GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:0048014; P:Tie signaling pathway; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR018941; Tyr_kin_Tie2_Ig-like_dom-1_N.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF00041; fn3; 3.
Pfam; PF10430; Ig_Tie2_1; 1.
Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00181; EGF; 2.
SMART; SM00060; FN3; 3.
SMART; SM00220; S_TKc; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00022; EGF_1; 3.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
ATP-binding; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
Disulfide bond; EGF-like domain; Glycoprotein; Immunoglobulin domain;
Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1..22
/evidence="ECO:0000250"
CHAIN 23..1122
/note="Angiopoietin-1 receptor"
/id="PRO_0000024475"
TOPO_DOM 23..746
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 747..767
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 768..1122
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 44..123
/note="Ig-like C2-type 1"
DOMAIN 210..252
/note="EGF-like 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 254..299
/note="EGF-like 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 301..341
/note="EGF-like 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
DOMAIN 350..440
/note="Ig-like C2-type 2"
DOMAIN 444..539
/note="Fibronectin type-III 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 543..635
/note="Fibronectin type-III 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 640..733
/note="Fibronectin type-III 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
DOMAIN 822..1094
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 828..836
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 962
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 853
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 858
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q02763"
MOD_RES 990
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:Q02763"
MOD_RES 1100
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000305|PubMed:12665569"
MOD_RES 1106
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:12665569"
CARBOHYD 140
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 158
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 399
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 438
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 464
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 558
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 595
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 648
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 690
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 44..102
/evidence="ECO:0000250"
DISULFID 211..220
/evidence="ECO:0000250"
DISULFID 224..233
/evidence="ECO:0000250"
DISULFID 227..240
/evidence="ECO:0000250"
DISULFID 242..251
/evidence="ECO:0000250"
DISULFID 255..264
/evidence="ECO:0000250"
DISULFID 268..274
/evidence="ECO:0000250"
DISULFID 280..287
/evidence="ECO:0000250"
DISULFID 289..298
/evidence="ECO:0000250"
DISULFID 302..311
/evidence="ECO:0000250"
DISULFID 315..323
/evidence="ECO:0000250"
DISULFID 317..329
/evidence="ECO:0000250"
DISULFID 331..340
/evidence="ECO:0000250"
DISULFID 370..424
/evidence="ECO:0000250"
MUTAGEN 853
/note="K->A: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:12665569,
ECO:0000269|PubMed:7958865"
MUTAGEN 1100
/note="Y->F: Reduced levels of autophosphorylation.
Abolishes interaction with GRB2 and GRB7. Abolishes
phosphorylation of GRB7 and PIK3R1."
/evidence="ECO:0000269|PubMed:10521483,
ECO:0000269|PubMed:12665569, ECO:0000269|PubMed:9632797"
MUTAGEN 1106
/note="Y->F: Reduced levels of autophosphorylation."
/evidence="ECO:0000269|PubMed:12665569"
CONFLICT 161..171
/note="FIHSVPRHEVP -> LHPLSAPGMKYL (in Ref. 3; BAA02883)"
/evidence="ECO:0000305"
CONFLICT 538
/note="S -> C (in Ref. 2; CAA47857)"
/evidence="ECO:0000305"
CONFLICT 736
/note="A -> G (in Ref. 2; CAA47857 and 4; AAB28663)"
/evidence="ECO:0000305"
CONFLICT 745..761
/note="MLLIAILGSAGMTCITV -> DATHSHPWVWNDFASPC (in Ref. 3;
BAA02883)"
/evidence="ECO:0000305"
CONFLICT 786
/note="N -> NV (in Ref. 3; BAA02883 and 6; no nucleotide
entry)"
/evidence="ECO:0000305"
CONFLICT 913
/note="R -> G (in Ref. 3; BAA02883)"
/evidence="ECO:0000305"
CONFLICT 925..931
/note="AIANSTA -> CHRQQYS (in Ref. 3; BAA02883)"
/evidence="ECO:0000305"
CONFLICT 1117
/note="S -> P (in Ref. 3; BAA02883)"
/evidence="ECO:0000305"
SEQUENCE 1122 AA; 125701 MW; F879623D103FFE96 CRC64;
MDSLAGLVLC GVSLLLYGVV EGAMDLILIN SLPLVSDAET SLTCIASGWH PHEPITIGRD
FEALMNQHQD PLEVTQDVTR EWAKKVVWKR EKASKINGAY FCEGRVRGQA IRIRTMKMRQ
QASFLPATLT MTVDRGDNVN ISFKKVLIKE EDAVIYKNGS FIHSVPRHEV PDILEVHLPH
AQPQDAGVYS ARYIGGNLFT SAFTRLIVRR CEAQKWGPDC SRPCTTCKNN GVCHEDTGEC
ICPPGFMGRT CEKACEPHTF GRTCKERCSG PEGCKSYVFC LPDPYGCSCA TGWRGLQCNE
ACPSGYYGPD CKLRCHCTNE EICDRFQGCL CSQGWQGLQC EKEGRPRMTP QIEDLPDHIE
VNSGKFNPIC KASGWPLPTS EEMTLVKPDG TVLQPNDFNY TDRFSVAIFT VNRVLPPDSG
VWVCSVNTVA GMVEKPFNIS VKVLPEPLHA PNVIDTGHNF AIINISSEPY FGDGPIKSKK
LFYKPVNQAW KYIEVTNEIF TLNYLEPRTD YELCVQLARP GEGGEGHPGP VRRFTTASIG
LPPPRGLSLL PKSQTALNLT WQPIFTNSED EFYVEVERRS LQTTSDQQNI KVPGNLTSVL
LSNLVPREQY TVRARVNTKA QGEWSEELRA WTLSDILPPQ PENIKISNIT DSTAMVSWTI
VDGYSISSII IRYKVQGKNE DQHIDVKIKN ATVTQYQLKG LEPETTYHVD IFAENNIGSS
NPAFSHELRT LPHSPASADL GGGKMLLIAI LGSAGMTCIT VLLAFLIMLQ LKRANVQRRM
AQAFQNREEP AVQFNSGTLA LNRKAKNNPD PTIYPVLDWN DIKFQDVIGE GNFGQVLKAR
IKKDGLRMDA AIKRMKEYAS KDDHRDFAGE LEVLCKLGHH PNIINLLGAC EHRGYLYLAI
EYAPHGNLLD FLRKSRVLET DPAFAIANST ASTLSSQQLL HFAADVARGM DYLSQKQFIH
RDLAARNILV GENYIAKIAD FGLSRGQEVY VKKTMGRLPV RWMAIESLNY SVYTTNSDVW
SYGVLLWEIV SLGGTPYCGM TCAELYEKLP QGYRLEKPLN CDDEVYDLMR QCWREKPYER
PSFAQILVSL NRMLEERKTY VNTTLYEKFT YAGIDCSAEE AA


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Related Genes :
[Tek Hyk Tie-2 Tie2] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (HYK) (STK1) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (mTIE2) (p140 TEK) (CD antigen CD202b)
[TEK TIE2 VMCM VMCM1] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (hTIE2) (p140 TEK) (CD antigen CD202b)
[TEK TIE-2 TIE2] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TIE-2) (CD antigen CD202b)
[tie2 tie-2] Tyrosine-protein kinase receptor Tie-2 (EC 2.7.10.1) (Tyrosine kinase with Ig and EGF homology domains-2)
[FLT3 CD135 FLK2 STK1] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase-2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Stem cell tyrosine kinase 1) (STK-1) (CD antigen CD135)
[KDR FLK1 VEGFR2] Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase insert domain receptor) (KDR) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
[FLT1 FLT FRT VEGFR1] Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase FRT) (Tyrosine-protein kinase receptor FLT) (FLT) (Vascular permeability factor receptor)
[Kdr Flk-1 Flk1] Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase NYK) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
[DDR1 CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)
[Flt1 Emrk2 Flt Vegfr1] Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Embryonic receptor kinase 2) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase receptor FLT)
[Kdr Flk1] Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Protein-tyrosine kinase receptor flk-1) (CD antigen CD309)
[kdr flk1b kdrb si:busm1-205d10.1 si:ch211-254j6.1] Vascular endothelial growth factor receptor 2 (VEGFR-2) (EC 2.7.10.1) (Fetal liver kinase 1b) (FLK-1b) (Kinase insert domain receptor) (Kinase insert domain receptor-B) (Protein-tyrosine kinase receptor flk-1b) (Vascular endothelial growth factor receptor 2 homolog B) (VEGFR-2 homolog B)
[Flt1 Flt-1 Vegfr1] Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase receptor FLT)
[kdrl flk flk-1 flk1 flka kdr kdra vegfr2 vegfr4 vegr2 si:ch211-276g21.4] Vascular endothelial growth factor receptor kdr-like (EC 2.7.10.1) (Fetal liver kinase 1) (FLK-1) (Kinase insert domain receptor-A) (Kinase insert domain receptor-like) (Protein-tyrosine kinase receptor flk-1) (Vascular endothelial growth factor receptor 4) (VEGFR-4)
[FLT4 VEGFR3] Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4)
[NTRK1 MTC TRK TRKA] High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1) (TRK1-transforming tyrosine kinase protein) (Tropomyosin-related kinase A) (Tyrosine kinase receptor) (Tyrosine kinase receptor A) (Trk-A) (gp140trk) (p140-TrkA)
[Flt4 Flt-4 Vegfr3] Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4)
[Flt4 Flt-4 Vegfr3] Vascular endothelial growth factor receptor 3 (VEGFR-3) (EC 2.7.10.1) (Fms-like tyrosine kinase 4) (FLT-4) (Tyrosine-protein kinase receptor FLT4)
[Epha2 Eck Myk2 Sek2] 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)
[Tek rCG_53516] Receptor protein-tyrosine kinase (EC 2.7.10.1)
[EPHB1 ELK EPHT2 HEK6 NET] Ephrin type-B receptor 1 (EC 2.7.10.1) (ELK) (EPH tyrosine kinase 2) (EPH-like kinase 6) (EK6) (hEK6) (Neuronally-expressed EPH-related tyrosine kinase) (NET) (Tyrosine-protein kinase receptor EPH-2)
[Ntrk1 Trk Trka] High affinity nerve growth factor receptor (EC 2.7.10.1) (Neurotrophic tyrosine kinase receptor type 1) (Slow nerve growth factor receptor) (p140-TrkA) (Trk-A)
[ERBB2 HER2 MLN19 NEU NGL] Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Metastatic lymph node gene 19 protein) (MLN 19) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (Tyrosine kinase-type cell surface receptor HER2) (p185erbB2) (CD antigen CD340)
[Ptk2b Fak2 Pyk2 Raftk] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[Flt3 Flk-2 Flt-3] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase 2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Tyrosine-protein kinase receptor flk-2) (CD antigen CD135)
[Ros1 Ros Ros-1] Proto-oncogene tyrosine-protein kinase ROS (EC 2.7.10.1) (Proto-oncogene c-Ros) (Proto-oncogene c-Ros-1) (Receptor tyrosine kinase c-ros oncogene 1) (c-Ros receptor tyrosine kinase)
[Ptprb] Receptor-type tyrosine-protein phosphatase beta (Protein-tyrosine phosphatase beta) (R-PTP-beta) (EC 3.1.3.48) (Vascular endothelial protein tyrosine phosphatase) (VE-PTP)
[EPHB2 DRT EPHT3 EPTH3 ERK HEK5 TYRO5] Ephrin type-B receptor 2 (EC 2.7.10.1) (Developmentally-regulated Eph-related tyrosine kinase) (ELK-related tyrosine kinase) (EPH tyrosine kinase 3) (EPH-like kinase 5) (EK5) (hEK5) (Renal carcinoma antigen NY-REN-47) (Tyrosine-protein kinase TYRO5) (Tyrosine-protein kinase receptor EPH-3) [Cleaved into: EphB2/CTF1; EphB2/CTF2]
[TEK] Receptor protein-tyrosine kinase (EC 2.7.10.1)
[TEK] Receptor protein-tyrosine kinase (EC 2.7.10.1)

Bibliography :