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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)

 TIE2_HUMAN              Reviewed;        1124 AA.
Q02763; A8K6W0; B4DH20; B4DHD3; D3DRK5; E7EWI2; Q5TCU2; Q8IV34;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
05-JUN-2019, entry version 211.
RecName: Full=Angiopoietin-1 receptor;
EC=2.7.10.1;
AltName: Full=Endothelial tyrosine kinase;
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=hTIE2;
AltName: Full=p140 TEK;
AltName: CD_antigen=CD202b;
Flags: Precursor;
Name=TEK; Synonyms=TIE2, VMCM, VMCM1;
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, TISSUE
SPECIFICITY, AND VARIANT PRO-346.
TISSUE=Placenta;
PubMed=8382358;
Ziegler S.F., Bird T.A., Schneringer J.A., Schooley K.A., Baum P.R.;
"Molecular cloning and characterization of a novel receptor protein
tyrosine kinase from human placenta.";
Oncogene 8:663-670(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANT PRO-346.
TISSUE=Brain, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-346.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-346.
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]
PROTEIN SEQUENCE OF 23-37.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
FUNCTION AS RECEPTOR FOR ANGPT1 AND ANGPT2, INTERACTION WITH ANGPT1
AND ANGPT2, AND AUTOPHOSPHORYLATION.
PubMed=9204896; DOI=10.1126/science.277.5322.55;
Maisonpierre P.C., Suri C., Jones P.F., Bartunkova S., Wiegand S.J.,
Radziejewski C., Compton D.L., McClain J., Aldrich T.H.,
Papadopoulos N., Daly T.J., Davis S., Sato T.N., Yancopoulos G.D.;
"Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo
angiogenesis.";
Science 277:55-60(1997).
[8]
SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND TISSUE SPECIFICITY.
PubMed=11806244; DOI=10.1023/A:1012226627813;
Reusch P., Barleon B., Weindel K., Martiny-Baron G., Godde A.,
Siemeister G., Marme D.;
"Identification of a soluble form of the angiopoietin receptor TIE-2
released from endothelial cells and present in human blood.";
Angiogenesis 4:123-131(2001).
[9]
CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION BY MASS
SPECTROMETRY, AND PHOSPHORYLATION AT TYR-860; TYR-992 AND TYR-1108.
PubMed=11513602; DOI=10.1021/bi010959e;
Murray B.W., Padrique E.S., Pinko C., McTigue M.A.;
"Mechanistic effects of autophosphorylation on receptor tyrosine
kinase catalysis: enzymatic characterization of Tie2 and phospho-
Tie2.";
Biochemistry 40:10243-10253(2001).
[10]
FUNCTION IN REGULATION OF PHOSPHATIDYLINOSITOL 3-KINASE ACTIVITY;
ENDOTHELIAL CELL MIGRATION AND REORGANIZATION OF THE ACTIN
CYTOSKELETON.
PubMed=12816861; DOI=10.1182/blood-2003-03-0670;
Cascone I., Audero E., Giraudo E., Napione L., Maniero F.,
Philips M.R., Collard J.G., Serini G., Bussolino F.;
"Tie-2-dependent activation of RhoA and Rac1 participates in
endothelial cell motility triggered by angiopoietin-1.";
Blood 102:2482-2490(2003).
[11]
INTERACTION WITH TNIP2, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF LYS-855.
PubMed=12609966; DOI=10.1161/01.RES.0000063422.38690.DC;
Hughes D.P., Marron M.B., Brindle N.P.;
"The antiinflammatory endothelial tyrosine kinase Tie2 interacts with
a novel nuclear factor-kappaB inhibitor ABIN-2.";
Circ. Res. 92:630-636(2003).
[12]
FUNCTION IN REGULATION OF ANGIOGENESIS; CELL SURVIVAL; CELL MIGRATION
AND ACTIVATION OF AKT1, DOMAIN, AND INTERACTION WITH ANGPT1; ANGPT2
AND ANGPT4.
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).
[13]
FUNCTION AS ANGPT1 RECEPTOR IN PHOSPHORYLATION OF SHC1 AND PIK3R1;
REGULATION OF CELL MIGRATION AND ANGIOGENESIS, AUTOPHOSPHORYLATION,
MUTAGENESIS OF TYR-1102, PHOSPHORYLATION AT TYR-1102, CATALYTIC
ACTIVITY, AND INTERACTION WITH SHC1.
PubMed=14665640; DOI=10.1074/jbc.M307456200;
Audero E., Cascone I., Maniero F., Napione L., Arese M.,
Lanfrancone L., Bussolino F.;
"Adaptor ShcA protein binds tyrosine kinase Tie2 receptor and
regulates migration and sprouting but not survival of endothelial
cells.";
J. Biol. Chem. 279:13224-13233(2004).
[14]
INTERACTION WITH TIE1, SUBCELLULAR LOCATION, FUNCTION AS RECEPTOR FOR
ANGPT1 IN PHOSPHORYLATION OF TIE1, AUTOPHOSPHORYLATION, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF LYS-855.
PubMed=15851516; DOI=10.1083/jcb.200411105;
Saharinen P., Kerkela K., Ekman N., Marron M., Brindle N., Lee G.M.,
Augustin H., Koh G.Y., Alitalo K.;
"Multiple angiopoietin recombinant proteins activate the Tie1 receptor
tyrosine kinase and promote its interaction with Tie2.";
J. Cell Biol. 169:239-243(2005).
[15]
FUNCTION AS ANGPT1 RECEPTOR IN ACTIVATION OF AKT1 OR MAPK1/ERK2 AND
MAPK3/ERK1; REGULATION OF ENDOTHELIAL CELL MIGRATION AND CELL
SPREADING, AND SUBCELLULAR LOCATION.
PubMed=18425120; DOI=10.1038/ncb1714;
Fukuhara S., Sako K., Minami T., Noda K., Kim H.Z., Kodama T.,
Shibuya M., Takakura N., Koh G.Y., Mochizuki N.;
"Differential function of Tie2 at cell-cell contacts and cell-
substratum contacts regulated by angiopoietin-1.";
Nat. Cell Biol. 10:513-526(2008).
[16]
FUNCTION AS ANGPT1 RECEPTOR IN ACTIVATION OF AKT1 OR MAPK1/ERK2 AND
MAPK3/ERK1; REGULATION OF ENDOTHELIAL CELL MIGRATION AND REGULATION OF
FOCAL ADHESION ASSEMBLY, INTERACTION WITH TIE1, AUTOPHOSPHORYLATION,
AND SUBCELLULAR LOCATION.
PubMed=18425119; DOI=10.1038/ncb1715;
Saharinen P., Eklund L., Miettinen J., Wirkkala R., Anisimov A.,
Winderlich M., Nottebaum A., Vestweber D., Deutsch U., Koh G.Y.,
Olsen B.R., Alitalo K.;
"Angiopoietins assemble distinct Tie2 signalling complexes in
endothelial cell-cell and cell-matrix contacts.";
Nat. Cell Biol. 10:527-537(2008).
[17]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPRB.
PubMed=19116766; DOI=10.1007/s10456-008-9126-0;
Yacyshyn O.K., Lai P.F.H., Forse K., Teichert-Kuliszewska K.,
Jurasz P., Stewart D.J.;
"Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in
human endothelial cells.";
Angiogenesis 12:25-33(2009).
[18]
INTERACTION WITH CBL, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=19689429; DOI=10.1042/BJ20091010;
Wehrle C., Van Slyke P., Dumont D.J.;
"Angiopoietin-1-induced ubiquitylation of Tie2 by c-Cbl is required
for internalization and degradation.";
Biochem. J. 423:375-380(2009).
[19]
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).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-596.
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).
[21]
FUNCTION AS RECEPTOR FOR ANGPT1 AND ANGPT2 IN ACTIVATION OF
PHOSPHATIDYLINOSITOL 3-KINASE AND AKT1; STIMULATION OF ENDOTHELIAL
CELL SURVIVAL AND MIGRATION, CATALYTIC ACTIVITY, AND
AUTOPHOSPHORYLATION.
PubMed=19223473; DOI=10.1128/MCB.01472-08;
Yuan H.T., Khankin E.V., Karumanchi S.A., Parikh S.M.;
"Angiopoietin 2 is a partial agonist/antagonist of Tie2 signaling in
the endothelium.";
Mol. Cell. Biol. 29:2011-2022(2009).
[22]
REVIEW ON FUNCTION; INTERACTION WITH EFFECTOR AND SCAFFOLDING
PROTEINS, AND ROLE IN DISEASE.
PubMed=18366015; DOI=10.14670/HH-23.773;
Martin V., Liu D., Fueyo J., Gomez-Manzano C.;
"Tie2: a journey from normal angiogenesis to cancer and beyond.";
Histol. Histopathol. 23:773-780(2008).
[23]
REVIEW ON SUBCELLULAR LOCATION AND CONTEXT-SPECIFIC SIGNALING.
PubMed=19293632; DOI=10.3858/emm.2009.41.3.016;
Fukuhara S., Sako K., Noda K., Nagao K., Miura K., Mochizuki N.;
"Tie2 is tied at the cell-cell contacts and to extracellular matrix by
angiopoietin-1.";
Exp. Mol. Med. 41:133-139(2009).
[24]
REVIEW.
PubMed=19234476; DOI=10.1038/nrm2639;
Augustin H.G., Koh G.Y., Thurston G., Alitalo K.;
"Control of vascular morphogenesis and homeostasis through the
angiopoietin-Tie system.";
Nat. Rev. Mol. Cell Biol. 10:165-177(2009).
[25]
REVIEW.
PubMed=20054809; DOI=10.14670/HH-25.387;
Fukuhara S., Sako K., Noda K., Zhang J., Minami M., Mochizuki N.;
"Angiopoietin-1/Tie2 receptor signaling in vascular quiescence and
angiogenesis.";
Histol. Histopathol. 25:387-396(2010).
[26]
REVIEW ON SIGNALING, ACTIVITY REGULATION, AND ROLE IN DISEASE.
PubMed=20651738; DOI=10.1038/nrc2894;
Huang H., Bhat A., Woodnutt G., Lappe R.;
"Targeting the ANGPT-TIE2 pathway in malignancy.";
Nat. Rev. Cancer 10:575-585(2010).
[27]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 808-1124, ACTIVE SITE,
ACTIVITY REGULATION, AND PREDICTION OF ATP-BINDING REGION.
PubMed=11080633; DOI=10.1016/S0969-2126(00)00516-5;
Shewchuk L.M., Hassell A.M., Ellis B., Holmes W.D., Davis R.,
Horne E.L., Kadwell S.H., McKee D.D., Moore J.T.;
"Structure of the Tie2 RTK domain: self-inhibition by the nucleotide
binding loop, activation loop, and C-terminal tail.";
Structure 8:1105-1113(2000).
[28]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 23-445 ALONE AND IN COMPLEX
WITH ANGPT2, GLYCOSYLATION AT ASN-140, AND DISULFIDE BONDS.
PubMed=16732286; DOI=10.1038/nsmb1101;
Barton W.A., Tzvetkova-Robev D., Miranda E.P., Kolev M.V.,
Rajashankar K.R., Himanen J.P., Nikolov D.B.;
"Crystal structures of the Tie2 receptor ectodomain and the
angiopoietin-2-Tie2 complex.";
Nat. Struct. Mol. Biol. 13:524-532(2006).
[29]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 808-1124 IN COMPLEX WITH
TRIAZINE DERIVATIVE, AND ACTIVITY REGULATION.
PubMed=17350837; DOI=10.1016/j.bmcl.2007.02.067;
Hodous B.L., Geuns-Meyer S.D., Hughes P.E., Albrecht B.K., Bellon S.,
Caenepeel S., Cee V.J., Chaffee S.C., Emery M., Fretland J.,
Gallant P., Gu Y., Johnson R.E., Kim J.L., Long A.M., Morrison M.,
Olivieri P.R., Patel V.F., Polverino A., Rose P., Wang L., Zhao H.;
"Synthesis, structural analysis, and SAR studies of triazine
derivatives as potent, selective Tie-2 inhibitors.";
Bioorg. Med. Chem. Lett. 17:2886-2889(2007).
[30]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 808-1124 IN COMPLEX WITH
TRIAZINE DERIVATIVE, AND ACTIVITY REGULATION.
PubMed=17253678; DOI=10.1021/jm061107l;
Hodous B.L., Geuns-Meyer S.D., Hughes P.E., Albrecht B.K., Bellon S.,
Bready J., Caenepeel S., Cee V.J., Chaffee S.C., Coxon A., Emery M.,
Fretland J., Gallant P., Gu Y., Hoffman D., Johnson R.E., Kendall R.,
Kim J.L., Long A.M., Morrison M., Olivieri P.R., Patel V.F.,
Polverino A., Rose P., Tempest P., Wang L., Whittington D.A., Zhao H.;
"Evolution of a highly selective and potent 2-(pyridin-2-yl)-1,3,5-
triazine Tie-2 kinase inhibitor.";
J. Med. Chem. 50:611-626(2007).
[31]
X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 802-1124 IN COMPLEX WITH
THIAZOLOPYRIMIDINE DERIVATIVE, AND ACTIVITY REGULATION.
PubMed=19854647; DOI=10.1016/j.bmcl.2009.10.001;
Luke R.W., Ballard P., Buttar D., Campbell L., Curwen J., Emery S.C.,
Griffen A.M., Hassall L., Hayter B.R., Jones C.D., McCoull W.,
Mellor M., Swain M.L., Tucker J.A.;
"Novel thienopyrimidine and thiazolopyrimidine kinase inhibitors with
activity against Tie-2 in vitro and in vivo.";
Bioorg. Med. Chem. Lett. 19:6670-6674(2009).
[32]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 808-1124 IN COMPLEX WITH
CEP11207.
Fedorov A.A., Fedorov E.V., Pauletti D., Meyer S.L., Hudkins R.L.,
Almo S.C.;
"Crystal structure of cytoplasmic kinase domain of Tie2 complexed with
inhibitor CEP11207.";
Submitted (JAN-2010) to the PDB data bank.
[33]
VARIANT VMCM TRP-849.
PubMed=8980225; DOI=10.1016/S0092-8674(00)81814-0;
Vikkula M., Boon L.M., Carraway K.L. III, Calvert J.T., Diamonti A.J.,
Goumnerov B., Pasyk K.A., Marchuk D.A., Warman M.L., Cantley L.C.,
Mulliken J.B., Olse B.R.;
"Vascular dysmorphogenesis caused by an activating mutation in the
receptor tyrosine kinase TIE2.";
Cell 87:1181-1190(1996).
[34]
VARIANTS VMCM TRP-849 AND SER-897.
PubMed=10369874; DOI=10.1093/hmg/8.7.1279;
Calvert J.T., Riney T.J., Kontos C.D., Cha E.H., Prieto V.G.,
Shea C.R., Berg J.N., Nevin N.C., Simpson S.A., Pasyk K.A.,
Speer M.C., Peters K.G., Marchuk D.A.;
"Allelic and locus heterogeneity in inherited venous malformations.";
Hum. Mol. Genet. 8:1279-1289(1999).
[35]
VARIANT [LARGE SCALE ANALYSIS] ASN-117.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[36]
VARIANTS [LARGE SCALE ANALYSIS] ASN-117; THR-148; VAL-226; ILE-486;
LEU-600; PHE-634; ILE-676; THR-724; ALA-883 AND VAL-1124.
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).
[37]
INVOLVEMENT IN VMCM, INVOLVEMENT IN DISEASE, SUBCELLULAR LOCATION,
CHARACTERIZATION OF VARIANTS VMCM TRP-849, VARIANTS HIS-897; PHE-897;
SER-897; PHE-914; CYS-915; LEU-915 AND ILE-917, CHARACTERIZATION OF
VARIANTS HIS-897; PHE-897; SER-897; PHE-914; CYS-915; LEU-915 AND
ILE-917, AND PHOSPHORYLATION AT TYR-1102.
PubMed=19079259; DOI=10.1038/ng.272;
Limaye N., Wouters V., Uebelhoer M., Tuominen M., Wirkkala R.,
Mulliken J.B., Eklund L., Boon L.M., Vikkula M.;
"Somatic mutations in angiopoietin receptor gene TEK cause solitary
and multiple sporadic venous malformations.";
Nat. Genet. 41:118-124(2009).
[38]
VARIANTS VMCM TRP-849; CYS-897; HIS-915; CYS-918; LEU-919; SER-925 AND
ASN-1100, AND CHARACTERIZATION OF VARIANTS VMCM TRP-849; SER-897;
HIS-915; CYS-918; LEU-919; SER-925 AND ASN-1100.
PubMed=19888299; DOI=10.1038/ejhg.2009.193;
Wouters V., Limaye N., Uebelhoer M., Irrthum A., Boon L.M.,
Mulliken J.B., Enjolras O., Baselga E., Berg J., Dompmartin A.,
Ivarsson S.A., Kangesu L., Lacassie Y., Murphy J., Teebi A.S.,
Penington A., Rieu P., Vikkula M.;
"Hereditary cutaneomucosal venous malformations are caused by TIE2
mutations with widely variable hyper-phosphorylating effects.";
Eur. J. Hum. Genet. 18:414-420(2010).
[39]
INVOLVEMENT IN GLC3E, VARIANTS GLC3E 19-THR--ARG-210 DEL; TYR-233;
ASN-294 AND CYS-611, CHARACTERIZATION OF VARIANTS GLC3E
19-THR--ARG-210 DEL; TYR-233; ASN-294 AND CYS-611, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF CYS-224.
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:12816861, ECO:0000269|PubMed:14665640,
ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:15851516,
ECO:0000269|PubMed:18366015, ECO:0000269|PubMed:18425119,
ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:19223473,
ECO:0000269|PubMed:20651738, ECO:0000269|PubMed:9204896}.
-!- 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:11513602, ECO:0000269|PubMed:12609966,
ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15851516,
ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:8382358};
-!- ACTIVITY REGULATION: Angiopoietin binding leads to receptor
dimerization and activation by autophosphorylation at Tyr-992 on
the kinase activation loop. Inhibited by staurosporine, K252a,
PP2, damnacanthal, SB203580, CEP-11207, CEP-11981 and CE-245677.
Inhibited by triazine, thienopyrimidine and thiazolopyrimidine
derivatives. {ECO:0000269|PubMed:11080633,
ECO:0000269|PubMed:11513602, ECO:0000269|PubMed:17253678,
ECO:0000269|PubMed:17350837, ECO:0000269|PubMed:19854647,
ECO:0000269|PubMed:20651738}.
-!- 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 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. Interacts (tyrosine
phosphorylated) with TNIP2. Interacts (tyrosine phosphorylated)
with SHC1 (via SH2 domain). {ECO:0000269|PubMed:12609966,
ECO:0000269|PubMed:14665640, ECO:0000269|PubMed:15284220,
ECO:0000269|PubMed:15851516, ECO:0000269|PubMed:16732286,
ECO:0000269|PubMed:17253678, ECO:0000269|PubMed:17350837,
ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:19451274,
ECO:0000269|PubMed:19689429, ECO:0000269|PubMed:19854647,
ECO:0000269|PubMed:9204896, ECO:0000269|Ref.32}.
-!- INTERACTION:
O15123:ANGPT2; NbExp=4; IntAct=EBI-2257090, EBI-2912111;
O15123-1:ANGPT2; NbExp=5; IntAct=EBI-2257090, EBI-15552475;
Q05209:PTPN12; NbExp=2; IntAct=EBI-2257090, EBI-2266035;
P23467:PTPRB; NbExp=3; IntAct=EBI-2257090, EBI-1265766;
P08575:PTPRC; NbExp=3; IntAct=EBI-2257090, EBI-1341;
Q12913:PTPRJ; NbExp=2; IntAct=EBI-2257090, EBI-2264500;
Q15262:PTPRK; NbExp=2; IntAct=EBI-2257090, EBI-474052;
Q16827:PTPRO; NbExp=2; IntAct=EBI-2257090, EBI-723739;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18425119,
ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:19079259,
ECO:0000269|PubMed:27270174}; Single-pass type I membrane protein.
Cell junction {ECO:0000269|PubMed:18425119,
ECO:0000269|PubMed:18425120, ECO:0000269|PubMed:27270174}. Cell
junction, focal adhesion {ECO:0000305|PubMed:19293632}. Cytoplasm,
cytoskeleton. Secreted {ECO:0000269|PubMed:11806244}.
Note=Recruited to cell-cell contacts in quiescent endothelial
cells (PubMed:18425120, PubMed:18425119). 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
(PubMed:11806244). {ECO:0000269|PubMed:11806244,
ECO:0000269|PubMed:18425119, ECO:0000269|PubMed:18425120}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q02763-1; Sequence=Displayed;
Name=2;
IsoId=Q02763-2; Sequence=VSP_042138;
Name=3;
IsoId=Q02763-3; Sequence=VSP_042137, VSP_042138, VSP_042139;
-!- TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells.
Proteolytic processing gives rise to a soluble extracellular
domain that is detected in blood plasma (at protein level).
Predominantly expressed in endothelial cells and their
progenitors, the angioblasts. Has been directly found in placenta
and lung, with a lower level in umbilical vein endothelial cells,
brain and kidney. {ECO:0000269|PubMed:11806244,
ECO:0000269|PubMed:8382358}.
-!- 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:0000269|PubMed:15284220}.
-!- PTM: Proteolytic processing leads to the shedding of the
extracellular domain (soluble TIE-2 alias sTIE-2).
{ECO:0000269|PubMed:11806244}.
-!- 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-992 in the kinase activation loop is phosphorylated first,
followed by autophosphorylation at Tyr-1108 and at additional
tyrosine residues. ANGPT1-induced phosphorylation is impaired
during hypoxia, due to increased expression of ANGPT2.
Phosphorylation is important for interaction with GRB14, PIK3R1
and PTPN11. Phosphorylation at Tyr-1102 is important for
interaction with SHC1, GRB2 and GRB7. Phosphorylation at Tyr-1108
is important for interaction with DOK2 and for coupling to
downstream signal transduction pathways in endothelial cells.
Dephosphorylated by PTPRB. {ECO:0000269|PubMed:11513602,
ECO:0000269|PubMed:14665640}.
-!- PTM: Ubiquitinated. The phosphorylated receptor is ubiquitinated
and internalized, leading to its degradation.
{ECO:0000269|PubMed:19689429}.
-!- DISEASE: Dominantly inherited venous malformations (VMCM)
[MIM:600195]: An error of vascular morphogenesis characterized by
dilated, serpiginous channels. {ECO:0000269|PubMed:10369874,
ECO:0000269|PubMed:19079259, ECO:0000269|PubMed:19888299,
ECO:0000269|PubMed:8980225}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Somatic mutations of TEK are associated with
solitary and multiple sporadic venous malformations.
{ECO:0000269|PubMed:19079259}.
-!- DISEASE: Note=May play a role in a range of diseases with a
vascular component, including neovascularization of tumors,
psoriasis and inflammation.
-!- DISEASE: Glaucoma 3, primary congenital, E (GLC3E) [MIM:617272]:
An autosomal dominant form of primary congenital glaucoma (PCG).
PCG is characterized by marked increase of intraocular pressure at
birth or early childhood, large ocular globes (buphthalmos) and
corneal edema. It results from developmental defects of the
trabecular meshwork and anterior chamber angle of the eye that
prevent adequate drainage of aqueous humor.
{ECO:0000269|PubMed:27270174}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Tie subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TEKID42517ch9p21.html";
-----------------------------------------------------------------------
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EMBL; L06139; AAA61139.1; -; mRNA.
EMBL; AK291775; BAF84464.1; -; mRNA.
EMBL; AK294887; BAG57981.1; -; mRNA.
EMBL; AK295043; BAG58094.1; -; mRNA.
EMBL; AL133411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL355433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58571.1; -; Genomic_DNA.
EMBL; CH471071; EAW58572.1; -; Genomic_DNA.
EMBL; BC035514; AAH35514.2; -; mRNA.
CCDS; CCDS6519.1; -. [Q02763-1]
CCDS; CCDS75825.1; -. [Q02763-2]
CCDS; CCDS78389.1; -. [Q02763-3]
PIR; I58388; I58388.
RefSeq; NP_000450.2; NM_000459.4.
RefSeq; NP_001277006.1; NM_001290077.1.
RefSeq; NP_001277007.1; NM_001290078.1.
PDB; 1FVR; X-ray; 2.20 A; A/B=808-1124.
PDB; 2GY5; X-ray; 2.90 A; A=23-445.
PDB; 2GY7; X-ray; 3.70 A; B=23-445.
PDB; 2OO8; X-ray; 2.20 A; X=808-1124.
PDB; 2OSC; X-ray; 2.80 A; A=808-1124.
PDB; 2P4I; X-ray; 2.50 A; A/B=808-1124.
PDB; 2WQB; X-ray; 2.95 A; A=802-1124.
PDB; 3BEA; X-ray; 2.02 A; A=917-935.
PDB; 3L8P; X-ray; 2.40 A; A=808-1124.
PDB; 4K0V; X-ray; 4.51 A; A=23-542.
PDB; 4X3J; X-ray; 2.50 A; A=802-1122.
PDB; 5MYA; X-ray; 2.90 A; A/B=443-742.
PDB; 5MYB; X-ray; 2.60 A; A/B=443-742.
PDB; 5UTK; X-ray; 2.50 A; A/B=442-741.
PDB; 6MWE; X-ray; 2.05 A; A/B=808-1124.
PDBsum; 1FVR; -.
PDBsum; 2GY5; -.
PDBsum; 2GY7; -.
PDBsum; 2OO8; -.
PDBsum; 2OSC; -.
PDBsum; 2P4I; -.
PDBsum; 2WQB; -.
PDBsum; 3BEA; -.
PDBsum; 3L8P; -.
PDBsum; 4K0V; -.
PDBsum; 4X3J; -.
PDBsum; 5MYA; -.
PDBsum; 5MYB; -.
PDBsum; 5UTK; -.
PDBsum; 6MWE; -.
SMR; Q02763; -.
BioGrid; 112869; 20.
DIP; DIP-6047N; -.
IntAct; Q02763; 22.
MINT; Q02763; -.
STRING; 9606.ENSP00000369375; -.
BindingDB; Q02763; -.
ChEMBL; CHEMBL4128; -.
DrugBank; DB00415; Ampicillin.
DrugBank; DB08221; N-{4-METHYL-3-[(3-PYRIMIDIN-4-YLPYRIDIN-2-YL)AMINO]PHENYL}-3-(TRIFLUOROMETHYL)BENZAMIDE.
DrugBank; DB08901; Ponatinib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB05294; Vandetanib.
DrugBank; DB05153; XL184.
GuidetoPHARMACOLOGY; 1842; -.
GlyConnect; 769; -.
iPTMnet; Q02763; -.
PhosphoSitePlus; Q02763; -.
UniCarbKB; Q02763; -.
BioMuta; TEK; -.
DMDM; 218511853; -.
EPD; Q02763; -.
jPOST; Q02763; -.
PaxDb; Q02763; -.
PeptideAtlas; Q02763; -.
PRIDE; Q02763; -.
ProteomicsDB; 58121; -.
ProteomicsDB; 58122; -. [Q02763-2]
ProteomicsDB; 58123; -. [Q02763-3]
DNASU; 7010; -.
Ensembl; ENST00000380036; ENSP00000369375; ENSG00000120156. [Q02763-1]
Ensembl; ENST00000406359; ENSP00000383977; ENSG00000120156. [Q02763-2]
Ensembl; ENST00000519097; ENSP00000430686; ENSG00000120156. [Q02763-3]
GeneID; 7010; -.
KEGG; hsa:7010; -.
UCSC; uc003zqi.5; human. [Q02763-1]
CTD; 7010; -.
DisGeNET; 7010; -.
GeneCards; TEK; -.
GeneReviews; TEK; -.
HGNC; HGNC:11724; TEK.
HPA; CAB010359; -.
HPA; HPA073265; -.
MalaCards; TEK; -.
MIM; 600195; phenotype.
MIM; 600221; gene.
MIM; 617272; phenotype.
neXtProt; NX_Q02763; -.
OpenTargets; ENSG00000120156; -.
Orphanet; 1059; Blue rubber bleb nevus.
Orphanet; 98976; Congenital glaucoma.
Orphanet; 2451; Mucocutaneous venous malformations.
PharmGKB; PA36441; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000158840; -.
HOGENOM; HOG000049232; -.
InParanoid; Q02763; -.
KO; K05121; -.
OMA; CEKEGMP; -.
OrthoDB; 1040796at2759; -.
PhylomeDB; Q02763; -.
TreeFam; TF317568; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
SignaLink; Q02763; -.
SIGNOR; Q02763; -.
ChiTaRS; TEK; human.
EvolutionaryTrace; Q02763; -.
GeneWiki; TEK_tyrosine_kinase; -.
GenomeRNAi; 7010; -.
PRO; PR:Q02763; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000120156; Expressed in 192 organ(s), highest expression level in metanephric glomerulus.
ExpressionAtlas; Q02763; baseline and differential.
Genevisible; Q02763; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IDA:HPA.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0060216; P:definitive hemopoiesis; TAS:UniProtKB.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0072012; P:glomerulus vasculature development; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0060347; P:heart trabecula formation; ISS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; TAS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; TAS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:1902533; P:positive regulation of intracellular signal transduction; IMP:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
GO; GO:2000351; P:regulation of endothelial cell apoptotic process; TAS:UniProtKB.
GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IMP:UniProtKB.
GO; GO:0043114; P:regulation of vascular permeability; TAS:UniProtKB.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002040; P:sprouting angiogenesis; IMP:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:0048014; P:Tie signaling pathway; IDA:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 6.
InterPro; IPR013032; EGF-like_CS.
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; Pkinase_Tyr; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00181; EGF; 3.
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;
3D-structure; Alternative splicing; Angiogenesis; ATP-binding;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disease mutation;
Disulfide bond; EGF-like domain; Glaucoma; Glycoprotein;
Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 22 {ECO:0000269|PubMed:15340161}.
CHAIN 23 1124 Angiopoietin-1 receptor.
/FTId=PRO_0000024474.
TOPO_DOM 23 748 Extracellular. {ECO:0000255}.
TRANSMEM 749 769 Helical. {ECO:0000255}.
TOPO_DOM 770 1124 Cytoplasmic. {ECO:0000255}.
DOMAIN 44 123 Ig-like C2-type 1.
DOMAIN 210 252 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 254 299 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 301 341 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 350 440 Ig-like C2-type 2.
DOMAIN 447 541 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 545 636 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 641 735 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 824 1096 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 830 838 ATP. {ECO:0000305}.
ACT_SITE 964 964 Proton acceptor.
{ECO:0000305|PubMed:11080633}.
BINDING 855 855 ATP. {ECO:0000305}.
MOD_RES 860 860 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11513602}.
MOD_RES 992 992 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11513602}.
MOD_RES 1102 1102 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:14665640,
ECO:0000269|PubMed:27270174}.
MOD_RES 1108 1108 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11513602}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16732286}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 560 560 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 596 596 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 649 649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 691 691 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 102 {ECO:0000269|PubMed:16732286}.
DISULFID 211 220 {ECO:0000269|PubMed:16732286}.
DISULFID 224 233 {ECO:0000269|PubMed:16732286}.
DISULFID 227 240 {ECO:0000269|PubMed:16732286}.
DISULFID 242 251 {ECO:0000269|PubMed:16732286}.
DISULFID 255 264 {ECO:0000269|PubMed:16732286}.
DISULFID 268 274 {ECO:0000269|PubMed:16732286}.
DISULFID 280 287 {ECO:0000269|PubMed:16732286}.
DISULFID 289 298 {ECO:0000269|PubMed:16732286}.
DISULFID 302 311 {ECO:0000269|PubMed:16732286}.
DISULFID 315 323 {ECO:0000269|PubMed:16732286}.
DISULFID 317 329 {ECO:0000269|PubMed:16732286}.
DISULFID 331 340 {ECO:0000269|PubMed:16732286}.
DISULFID 370 424 {ECO:0000269|PubMed:16732286}.
VAR_SEQ 18 121 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042137.
VAR_SEQ 300 342 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042138.
VAR_SEQ 788 788 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042139.
VARIANT 19 210 Missing (in GLC3E; formation of protein
aggregates).
{ECO:0000269|PubMed:27270174}.
/FTId=VAR_078045.
VARIANT 117 117 K -> N (in breast cancer samples;
infiltrating ductal carcinoma; somatic
mutation). {ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_035714.
VARIANT 148 148 I -> T (in dbSNP:rs35969327).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041855.
VARIANT 226 226 A -> V (in dbSNP:rs35814893).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041856.
VARIANT 233 233 C -> Y (in GLC3E; enhanced proteasomal
degradation).
{ECO:0000269|PubMed:27270174}.
/FTId=VAR_078046.
VARIANT 294 294 K -> N (in GLC3E; unknown pathological
significance; 10-fold decrease of Tyr-
1102 phosphorylation; no effect on
membrane location; dbSNP:rs146169480).
{ECO:0000269|PubMed:27270174}.
/FTId=VAR_078047.
VARIANT 346 346 Q -> P (in dbSNP:rs682632).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8382358,
ECO:0000269|Ref.4}.
/FTId=VAR_048002.
VARIANT 391 391 T -> I (in dbSNP:rs34032300).
/FTId=VAR_048003.
VARIANT 486 486 V -> I (in dbSNP:rs1334811).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_024578.
VARIANT 600 600 V -> L (in dbSNP:rs35030851).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041857.
VARIANT 611 611 Y -> C (in GLC3E; reduced response to
ligand; loss of ligand-induced
phosphorylation; no effect on basal
membrane location; dbSNP:rs1306527531).
{ECO:0000269|PubMed:27270174}.
/FTId=VAR_078048.
VARIANT 634 634 L -> F (in dbSNP:rs35378598).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041858.
VARIANT 676 676 V -> I (in dbSNP:rs56367117).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041859.
VARIANT 724 724 A -> T (in dbSNP:rs4631561).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041860.
VARIANT 849 849 R -> W (in VMCM; increased ligand-
independent autophosphorylation and
kinase activation; no effect on location
at membrane; dbSNP:rs80338908).
{ECO:0000269|PubMed:10369874,
ECO:0000269|PubMed:19079259,
ECO:0000269|PubMed:19888299,
ECO:0000269|PubMed:8980225}.
/FTId=VAR_006352.
VARIANT 883 883 P -> A (in an ovarian serous carcinoma
sample; somatic mutation;
dbSNP:rs1490428165).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041861.
VARIANT 897 897 Y -> C (in VMCM; increased ligand-
independent autophosphorylation and
kinase activation; dbSNP:rs80338909).
{ECO:0000269|PubMed:19888299}.
/FTId=VAR_066606.
VARIANT 897 897 Y -> F (found in a patient with multiple
sporadic venous malformations; increased
ligand-independent autophosphorylation;
the hyperphosphorylation increases when
associated with Leu-915).
{ECO:0000269|PubMed:19079259}.
/FTId=VAR_078049.
VARIANT 897 897 Y -> H (found in a patient with solitary
sporadic venous malformations; increased
ligand-independent autophosphorylation).
{ECO:0000269|PubMed:19079259}.
/FTId=VAR_078050.
VARIANT 897 897 Y -> S (in VMCM; also found in a patient
with solitary sporadic venous
malformations; increased ligand-
independent autophosphorylation and
kinase activation; dbSNP:rs80338909).
{ECO:0000269|PubMed:10369874,
ECO:0000269|PubMed:19079259,
ECO:0000269|PubMed:19888299}.
/FTId=VAR_008716.
VARIANT 914 914 L -> F (found in patients with solitary
and multiple sporadic venous
malformations; increased ligand-
independent autophosphorylation; novel
location at endoplasmic reticulum and
Golgi apparatus; partially retained at
endoplasmic reticulum and Golgi
apparatus).
{ECO:0000269|PubMed:19079259}.
/FTId=VAR_078051.
VARIANT 915 915 R -> C (found in a patient with solitary
sporadic venous malformations; increased
ligand-independent autophosphorylation).
{ECO:0000269|PubMed:19079259}.
/FTId=VAR_078052.
VARIANT 915 915 R -> H (in VMCM; strongly increased
ligand-independent autophosphorylation
and kinase activation;
dbSNP:rs387906745).
{ECO:0000269|PubMed:19888299}.
/FTId=VAR_066607.
VARIANT 915 915 R -> L (found in a patient with multiple
sporadic venous malformations; increased
ligand-independent autophosphorylation;
the autophosphorylation increases when
associated with Phe-897).
{ECO:0000269|PubMed:19079259}.
/FTId=VAR_078053.
VARIANT 917 917 S -> I (found in a patient with solitary
sporadic venous malformations; increased
ligand-independent autophosphorylation).
{ECO:0000269|PubMed:19079259}.
/FTId=VAR_078054.
VARIANT 918 918 R -> C (in VMCM; strongly increased
ligand-independent autophosphorylation
and kinase activation).
{ECO:0000269|PubMed:19888299}.
/FTId=VAR_066608.
VARIANT 919 919 V -> L (in VMCM; increased ligand-
independent autophosphorylation and
kinase activation).
{ECO:0000269|PubMed:19888299}.
/FTId=VAR_066609.
VARIANT 925 925 A -> S (in VMCM; increased ligand-
independent autophosphorylation and
kinase activation).
{ECO:0000269|PubMed:19888299}.
/FTId=VAR_066610.
VARIANT 1100 1100 K -> N (in VMCM; strongly increased
ligand-independent autophosphorylation
and kinase activation).
{ECO:0000269|PubMed:19888299}.
/FTId=VAR_066611.
VARIANT 1124 1124 A -> V (in a renal clear cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041862.
MUTAGEN 224 224 C->S: Reduces protein abundance.
{ECO:0000269|PubMed:27270174}.
MUTAGEN 855 855 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:12609966,
ECO:0000269|PubMed:15851516}.
MUTAGEN 1102 1102 Y->F: Abolishes interaction with SHC1.
{ECO:0000269|PubMed:14665640}.
CONFLICT 536 536 F -> L (in Ref. 2; BAG58094).
{ECO:0000305}.
CONFLICT 695 695 T -> I (in Ref. 1; AAA61139).
{ECO:0000305}.
CONFLICT 939 940 QQ -> HH (in Ref. 5; AAH35514).
{ECO:0000305}.
STRAND 26 29 {ECO:0000244|PDB:2GY5}.
STRAND 33 35 {ECO:0000244|PDB:2GY5}.
STRAND 40 46 {ECO:0000244|PDB:2GY5}.
STRAND 56 59 {ECO:0000244|PDB:2GY5}.
TURN 61 63 {ECO:0000244|PDB:2GY5}.
STRAND 64 66 {ECO:0000244|PDB:2GY5}.
STRAND 74 76 {ECO:0000244|PDB:2GY5}.
STRAND 80 88 {ECO:0000244|PDB:2GY5}.
STRAND 98 106 {ECO:0000244|PDB:2GY5}.
STRAND 109 119 {ECO:0000244|PDB:2GY5}.
STRAND 123 125 {ECO:0000244|PDB:2GY5}.
STRAND 127 133 {ECO:0000244|PDB:2GY5}.
STRAND 139 145 {ECO:0000244|PDB:2GY5}.
STRAND 153 157 {ECO:0000244|PDB:2GY5}.
STRAND 160 165 {ECO:0000244|PDB:2GY5}.
HELIX 167 169 {ECO:0000244|PDB:2GY5}.
STRAND 172 178 {ECO:0000244|PDB:2GY5}.
HELIX 183 185 {ECO:0000244|PDB:2GY5}.
STRAND 187 193 {ECO:0000244|PDB:2GY5}.
HELIX 198 200 {ECO:0000244|PDB:2GY5}.
STRAND 202 208 {ECO:0000244|PDB:2GY5}.
STRAND 215 217 {ECO:0000244|PDB:2GY5}.
TURN 235 237 {ECO:0000244|PDB:2GY5}.
STRAND 246 248 {ECO:0000244|PDB:2GY5}.
STRAND 259 261 {ECO:0000244|PDB:2GY5}.
TURN 271 276 {ECO:0000244|PDB:2GY5}.
STRAND 279 281 {ECO:0000244|PDB:2GY5}.
TURN 282 285 {ECO:0000244|PDB:2GY5}.
STRAND 286 288 {ECO:0000244|PDB:2GY5}.
HELIX 296 298 {ECO:0000244|PDB:2GY5}.
STRAND 322 324 {ECO:0000244|PDB:2GY5}.
TURN 325 327 {ECO:0000244|PDB:2GY5}.
STRAND 328 330 {ECO:0000244|PDB:2GY5}.
STRAND 361 366 {ECO:0000244|PDB:2GY5}.
STRAND 369 373 {ECO:0000244|PDB:2GY5}.
HELIX 380 382 {ECO:0000244|PDB:2GY5}.
STRAND 383 386 {ECO:0000244|PDB:2GY5}.
STRAND 396 400 {ECO:0000244|PDB:2GY5}.
STRAND 405 408 {ECO:0000244|PDB:2GY5}.
STRAND 411 414 {ECO:0000244|PDB:2GY5}.
HELIX 416 418 {ECO:0000244|PDB:2GY5}.
STRAND 420 428 {ECO:0000244|PDB:2GY5}.
STRAND 431 439 {ECO:0000244|PDB:2GY5}.
STRAND 446 449 {ECO:0000244|PDB:5UTK}.
STRAND 452 456 {ECO:0000244|PDB:5UTK}.
STRAND 461 464 {ECO:0000244|PDB:5UTK}.
STRAND 469 472 {ECO:0000244|PDB:5UTK}.
STRAND 476 485 {ECO:0000244|PDB:5UTK}.
STRAND 493 504 {ECO:0000244|PDB:5UTK}.
STRAND 512 521 {ECO:0000244|PDB:5UTK}.
STRAND 534 537 {ECO:0000244|PDB:5UTK}.
STRAND 550 553 {ECO:0000244|PDB:5UTK}.
STRAND 555 557 {ECO:0000244|PDB:5UTK}.
STRAND 559 562 {ECO:0000244|PDB:5UTK}.
STRAND 569 572 {ECO:0000244|PDB:5MYA}.
STRAND 575 581 {ECO:0000244|PDB:5UTK}.
STRAND 589 594 {ECO:0000244|PDB:5UTK}.
STRAND 598 602 {ECO:0000244|PDB:5UTK}.
STRAND 610 621 {ECO:0000244|PDB:5UTK}.
STRAND 629 632 {ECO:0000244|PDB:5UTK}.
STRAND 643 648 {ECO:0000244|PDB:5UTK}.
STRAND 655 660 {ECO:0000244|PDB:5UTK}.
STRAND 669 676 {ECO:0000244|PDB:5UTK}.
STRAND 685 689 {ECO:0000244|PDB:5UTK}.
STRAND 696 699 {ECO:0000244|PDB:5UTK}.
STRAND 707 715 {ECO:0000244|PDB:5UTK}.
STRAND 724 730 {ECO:0000244|PDB:5UTK}.
STRAND 816 818 {ECO:0000244|PDB:1FVR}.
HELIX 821 823 {ECO:0000244|PDB:6MWE}.
STRAND 824 833 {ECO:0000244|PDB:6MWE}.
STRAND 836 845 {ECO:0000244|PDB:6MWE}.
STRAND 848 857 {ECO:0000244|PDB:6MWE}.
HELIX 864 866 {ECO:0000244|PDB:2P4I}.
HELIX 872 879 {ECO:0000244|PDB:6MWE}.
STRAND 888 894 {ECO:0000244|PDB:6MWE}.
STRAND 897 903 {ECO:0000244|PDB:6MWE}.
HELIX 910 916 {ECO:0000244|PDB:6MWE}.
HELIX 919 922 {ECO:0000244|PDB:6MWE}.
HELIX 924 929 {ECO:0000244|PDB:6MWE}.
STRAND 932 936 {ECO:0000244|PDB:2OO8}.
HELIX 938 957 {ECO:0000244|PDB:6MWE}.
HELIX 967 969 {ECO:0000244|PDB:6MWE}.
STRAND 970 972 {ECO:0000244|PDB:6MWE}.
HELIX 974 976 {ECO:0000244|PDB:6MWE}.
STRAND 978 980 {ECO:0000244|PDB:6MWE}.
HELIX 985 987 {ECO:0000244|PDB:6MWE}.
HELIX 1000 1004 {ECO:0000244|PDB:6MWE}.
HELIX 1007 1012 {ECO:0000244|PDB:6MWE}.
HELIX 1017 1032 {ECO:0000244|PDB:6MWE}.
TURN 1038 1041 {ECO:0000244|PDB:6MWE}.
HELIX 1044 1050 {ECO:0000244|PDB:6MWE}.
HELIX 1051 1053 {ECO:0000244|PDB:6MWE}.
HELIX 1065 1074 {ECO:0000244|PDB:6MWE}.
HELIX 1079 1081 {ECO:0000244|PDB:6MWE}.
HELIX 1085 1097 {ECO:0000244|PDB:6MWE}.
STRAND 1098 1100 {ECO:0000244|PDB:6MWE}.
HELIX 1118 1120 {ECO:0000244|PDB:6MWE}.
SEQUENCE 1124 AA; 125830 MW; E739DEC3E4FEB124 CRC64;
MDSLASLVLC GVSLLLSGTV EGAMDLILIN SLPLVSDAET SLTCIASGWR PHEPITIGRD
FEALMNQHQD PLEVTQDVTR EWAKKVVWKR EKASKINGAY FCEGRVRGEA IRIRTMKMRQ
QASFLPATLT MTVDKGDNVN ISFKKVLIKE EDAVIYKNGS FIHSVPRHEV PDILEVHLPH
AQPQDAGVYS ARYIGGNLFT SAFTRLIVRR CEAQKWGPEC NHLCTACMNN GVCHEDTGEC
ICPPGFMGRT CEKACELHTF GRTCKERCSG QEGCKSYVFC LPDPYGCSCA TGWKGLQCNE
ACHPGFYGPD CKLRCSCNNG EMCDRFQGCL CSPGWQGLQC EREGIQRMTP KIVDLPDHIE
VNSGKFNPIC KASGWPLPTN EEMTLVKPDG TVLHPKDFNH TDHFSVAIFT IHRILPPDSG
VWVCSVNTVA GMVEKPFNIS VKVLPKPLNA PNVIDTGHNF AVINISSEPY FGDGPIKSKK
LLYKPVNHYE AWQHIQVTNE IVTLNYLEPR TEYELCVQLV RRGEGGEGHP GPVRRFTTAS
IGLPPPRGLN LLPKSQTTLN LTWQPIFPSS EDDFYVEVER RSVQKSDQQN IKVPGNLTSV
LLNNLHPREQ YVVRARVNTK AQGEWSEDLT AWTLSDILPP QPENIKISNI THSSAVISWT
ILDGYSISSI TIRYKVQGKN EDQHVDVKIK NATITQYQLK GLEPETAYQV DIFAENNIGS
SNPAFSHELV TLPESQAPAD LGGGKMLLIA ILGSAGMTCL TVLLAFLIIL QLKRANVQRR
MAQAFQNVRE EPAVQFNSGT LALNRKVKNN PDPTIYPVLD WNDIKFQDVI GEGNFGQVLK
ARIKKDGLRM DAAIKRMKEY ASKDDHRDFA GELEVLCKLG HHPNIINLLG ACEHRGYLYL
AIEYAPHGNL LDFLRKSRVL ETDPAFAIAN STASTLSSQQ LLHFAADVAR GMDYLSQKQF
IHRDLAARNI LVGENYVAKI ADFGLSRGQE VYVKKTMGRL PVRWMAIESL NYSVYTTNSD
VWSYGVLLWE IVSLGGTPYC GMTCAELYEK LPQGYRLEKP LNCDDEVYDL MRQCWREKPY
ERPSFAQILV SLNRMLEERK TYVNTTLYEK FTYAGIDCSA EEAA


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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
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
E0147r ELISA kit Flt1,FLT-1,Flt-1,Fms-like tyrosine kinase 1,Rat,Rattus norvegicus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
U0147r CLIA Flt1,FLT-1,Flt-1,Fms-like tyrosine kinase 1,Rat,Rattus norvegicus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 96T
E0147r ELISA Flt1,FLT-1,Flt-1,Fms-like tyrosine kinase 1,Rat,Rattus norvegicus,Tyrosine-protein kinase receptor FLT,Vascular endothelial growth factor receptor 1,VEGFR-1 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
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 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
U2227h CLIA kit BMX,Bone marrow tyrosine kinase gene in chromosome X protein,Cytoplasmic tyrosine-protein kinase BMX,Epithelial and endothelial tyrosine kinase,ETK,Homo sapiens,Human,NTK38 96T
Pathways :
WP1493: Carbon assimilation C4 pathway
WP1714: Tyrosine metabolism
WP1567: Glycolysis and Gluconeogenesis
WP253: Glycolysis
WP2292: Chemokine signaling pathway
WP1619: Amino sugar and nucleotide sugar metabolism
WP32: Translation Factors
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1653: Galactose metabolism
WP1703: Streptomycin biosynthesis
WP2272: Pathogenic Escherichia coli infection
WP1681: Pantothenate and CoA biosynthesis
WP1946: Cori Cycle
WP2328: Allograft rejection
WP1844: MAP kinase cascade
WP1701: Starch and sucrose metabolism
WP780: T Cell Receptor Signaling Pathway
WP27: Phenylalanine, Tyrosine, Tryptophan biosynthesis
WP1687: Phenylalanine, tyrosine and tryptophan biosynthesi
WP1144: B Cell Receptor Signaling Pathway
WP1011: T Cell Receptor Signaling Pathway
WP1345: T Cell Receptor Signaling Pathway
WP1869: Neuroransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell
WP352: T Cell Receptor Signaling Pathway

Related Genes :
[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 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 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)
[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)
[Tek rCG_53516] Endothelial-specific receptor tyrosine kinase (TEK receptor tyrosine kinase)
[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)
[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)
[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)
[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)
[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)
[Tek mCG_122568] Angiopoietin-1 receptor (Endothelial-specific receptor tyrosine kinase, isoform CRA_a)
[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)
[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)
[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)
[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)
[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)
[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]
[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)
[DDR1 EDDR1] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Discoidin receptor tyrosine kinase) (Tyrosine kinase DDR) (CD antigen CD167a)
[FGFR1 BFGFR CEK FGFBR FLG FLT2 HBGFR] Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331)

Bibliography :