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Q02858 (TIE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiopoietin-1 receptor

EC=2.7.10.1
Alternative name(s):
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
Short name=mTIE2
p140 TEK
CD_antigen=CD202b
Gene names
Name:Tek
Synonyms:Hyk, Tie-2, Tie2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1122 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.18

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.8

Enzyme regulation

Angiopoietin binding leads to receptor dimerization and activation by autophosphorylation at Tyr-990 on the kinase activation loop By similarity.

Subunit structure

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. Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Cell membrane; Single-pass type I membrane protein. Cell junction By similarity. Cell junctionfocal adhesion By similarity. Cytoplasmcytoskeleton By similarity. Secreted By similarity. 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.

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. Ref.6

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 By similarity. Ref.14

Post-translational modification

Proteolytic processing leads to the shedding of the extracellular domain (soluble TIE-2 alias sTIE-2) By similarity.

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. Ref.12 Ref.15 Ref.16

Ubiquitinated. The phosphorylated receptor is ubiquitinated and internalized, leading to its degradation By similarity. Ref.12 Ref.15 Ref.16

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. Ref.8 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily.

Contains 3 EGF-like domains.

Contains 3 fibronectin type-III domains.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Secreted
   DomainEGF-like domain
Immunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processTie signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

angiogenesis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

cell-cell adhesion

Inferred from mutant phenotype PubMed 9683559. Source: MGI

cell-matrix adhesion

Inferred from mutant phenotype PubMed 9683559. Source: MGI

endothelial cell proliferation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

heart development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

heart trabecula formation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

hemopoiesis

Inferred from mutant phenotype PubMed 15260986PubMed 9846489. Source: MGI

negative regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from genetic interaction PubMed 19409199. Source: MGI

negative regulation of endothelial cell apoptotic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

patterning of blood vessels

Traceable author statement PubMed 20299672. Source: DFLAT

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell adhesion

Inferred from mutant phenotype PubMed 15260986. Source: MGI

positive regulation of endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from genetic interaction PubMed 19409199. Source: MGI

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vascular endothelial growth factor receptor signaling pathway

Traceable author statement PubMed 20406889. Source: DFLAT

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of angiogenesis

Inferred from mutant phenotype PubMed 9683559. Source: MGI

regulation of cell migration

Inferred from mutant phenotype PubMed 9683559. Source: MGI

regulation of endothelial cell proliferation

Traceable author statement PubMed 20406889. Source: DFLAT

regulation of establishment or maintenance of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

response to retinoic acid

Inferred from direct assay PubMed 18439490. Source: BHF-UCL

sprouting angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

vasculogenesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from sequence model Ref.1. Source: MGI

integral component of plasma membrane

Inferred from electronic annotation. Source: InterPro

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein tyrosine kinase activity

Inferred from direct assay Ref.8. Source: UniProtKB

receptor activity

Inferred from physical interaction PubMed 8980223. Source: MGI

transmembrane receptor protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 11221100Angiopoietin-1 receptor
PRO_0000024475

Regions

Topological domain23 – 746724Extracellular Potential
Transmembrane747 – 76721Helical; Potential
Topological domain768 – 1122355Cytoplasmic Potential
Domain44 – 12380Ig-like C2-type 1
Domain210 – 25243EGF-like 1
Domain254 – 29946EGF-like 2
Domain301 – 34141EGF-like 3
Domain350 – 44091Ig-like C2-type 2
Domain444 – 53996Fibronectin type-III 1
Domain543 – 63593Fibronectin type-III 2
Domain640 – 73394Fibronectin type-III 3
Domain822 – 1094273Protein kinase
Nucleotide binding828 – 8369ATP By similarity

Sites

Active site9621Proton acceptor By similarity
Binding site8531ATP By similarity

Amino acid modifications

Modified residue8581Phosphotyrosine; by autocatalysis By similarity
Modified residue9901Phosphotyrosine; by autocatalysis By similarity
Modified residue11001Phosphotyrosine; by autocatalysis Probable
Modified residue11061Phosphotyrosine; by autocatalysis Ref.15
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation3991N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation5581N-linked (GlcNAc...) Potential
Glycosylation5951N-linked (GlcNAc...) Potential
Glycosylation6481N-linked (GlcNAc...) Potential
Glycosylation6901N-linked (GlcNAc...) Potential
Disulfide bond44 ↔ 102 By similarity
Disulfide bond211 ↔ 220 By similarity
Disulfide bond224 ↔ 233 By similarity
Disulfide bond227 ↔ 240 By similarity
Disulfide bond242 ↔ 251 By similarity
Disulfide bond255 ↔ 264 By similarity
Disulfide bond268 ↔ 274 By similarity
Disulfide bond280 ↔ 287 By similarity
Disulfide bond289 ↔ 298 By similarity
Disulfide bond302 ↔ 311 By similarity
Disulfide bond315 ↔ 323 By similarity
Disulfide bond317 ↔ 329 By similarity
Disulfide bond331 ↔ 340 By similarity
Disulfide bond370 ↔ 424 By similarity

Experimental info

Mutagenesis8531K → A: Loss of kinase activity. Ref.8 Ref.15
Mutagenesis11001Y → F: Reduced levels of autophosphorylation. Abolishes interaction with GRB2 and GRB7. Abolishes phosphorylation of GRB7 and PIK3R1. Ref.10 Ref.11 Ref.15
Mutagenesis11061Y → F: Reduced levels of autophosphorylation. Ref.15
Sequence conflict161 – 17111FIHSVPRHEVP → LHPLSAPGMKYL in BAA02883. Ref.3
Sequence conflict5381S → C in CAA47857. Ref.2
Sequence conflict7361A → G in CAA47857. Ref.2
Sequence conflict7361A → G in AAB28663. Ref.4
Sequence conflict745 – 76117MLLIA…TCITV → DATHSHPWVWNDFASPC in BAA02883. Ref.3
Sequence conflict7861N → NV in BAA02883. Ref.3
Sequence conflict7861N → NV no nucleotide entry Ref.6
Sequence conflict9131R → G in BAA02883. Ref.3
Sequence conflict925 – 9317AIANSTA → CHRQQYS in BAA02883. Ref.3
Sequence conflict11171S → P in BAA02883. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q02858 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: F879623D103FFE96

FASTA1,122125,701
        10         20         30         40         50         60 
MDSLAGLVLC GVSLLLYGVV EGAMDLILIN SLPLVSDAET SLTCIASGWH PHEPITIGRD 

        70         80         90        100        110        120 
FEALMNQHQD PLEVTQDVTR EWAKKVVWKR EKASKINGAY FCEGRVRGQA IRIRTMKMRQ 

       130        140        150        160        170        180 
QASFLPATLT MTVDRGDNVN ISFKKVLIKE EDAVIYKNGS FIHSVPRHEV PDILEVHLPH 

       190        200        210        220        230        240 
AQPQDAGVYS ARYIGGNLFT SAFTRLIVRR CEAQKWGPDC SRPCTTCKNN GVCHEDTGEC 

       250        260        270        280        290        300 
ICPPGFMGRT CEKACEPHTF GRTCKERCSG PEGCKSYVFC LPDPYGCSCA TGWRGLQCNE 

       310        320        330        340        350        360 
ACPSGYYGPD CKLRCHCTNE EICDRFQGCL CSQGWQGLQC EKEGRPRMTP QIEDLPDHIE 

       370        380        390        400        410        420 
VNSGKFNPIC KASGWPLPTS EEMTLVKPDG TVLQPNDFNY TDRFSVAIFT VNRVLPPDSG 

       430        440        450        460        470        480 
VWVCSVNTVA GMVEKPFNIS VKVLPEPLHA PNVIDTGHNF AIINISSEPY FGDGPIKSKK 

       490        500        510        520        530        540 
LFYKPVNQAW KYIEVTNEIF TLNYLEPRTD YELCVQLARP GEGGEGHPGP VRRFTTASIG 

       550        560        570        580        590        600 
LPPPRGLSLL PKSQTALNLT WQPIFTNSED EFYVEVERRS LQTTSDQQNI KVPGNLTSVL 

       610        620        630        640        650        660 
LSNLVPREQY TVRARVNTKA QGEWSEELRA WTLSDILPPQ PENIKISNIT DSTAMVSWTI 

       670        680        690        700        710        720 
VDGYSISSII IRYKVQGKNE DQHIDVKIKN ATVTQYQLKG LEPETTYHVD IFAENNIGSS 

       730        740        750        760        770        780 
NPAFSHELRT LPHSPASADL GGGKMLLIAI LGSAGMTCIT VLLAFLIMLQ LKRANVQRRM 

       790        800        810        820        830        840 
AQAFQNREEP AVQFNSGTLA LNRKAKNNPD PTIYPVLDWN DIKFQDVIGE GNFGQVLKAR 

       850        860        870        880        890        900 
IKKDGLRMDA AIKRMKEYAS KDDHRDFAGE LEVLCKLGHH PNIINLLGAC EHRGYLYLAI 

       910        920        930        940        950        960 
EYAPHGNLLD FLRKSRVLET DPAFAIANST ASTLSSQQLL HFAADVARGM DYLSQKQFIH 

       970        980        990       1000       1010       1020 
RDLAARNILV GENYIAKIAD FGLSRGQEVY VKKTMGRLPV RWMAIESLNY SVYTTNSDVW 

      1030       1040       1050       1060       1070       1080 
SYGVLLWEIV SLGGTPYCGM TCAELYEKLP QGYRLEKPLN CDDEVYDLMR QCWREKPYER 

      1090       1100       1110       1120 
PSFAQILVSL NRMLEERKTY VNTTLYEKFT YAGIDCSAEE AA 

« Hide

References

[1]"Tie-1 and tie-2 define another class of putative receptor tyrosine kinase genes expressed in early embryonic vascular system."
Sato T.N., Qin Y., Kozak C.A., Andus K.L.
Proc. Natl. Acad. Sci. U.S.A. 90:9355-9358(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Lung.
[2]"The endothelial-specific receptor tyrosine kinase, tek, is a member of a new subfamily of receptors."
Dumont D.J., Gradwol G.J., Fong G.-H., Auerbach R., Breitman M.L.
Oncogene 8:1293-1301(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
Tissue: Embryonic heart.
[3]"A novel tyrosine kinase, hyk, expressed in murine embryonic stem cells."
Horita K., Yagi T., Kohmura N., Tomooka Y., Ikawa Y., Aizawa S.
Biochem. Biophys. Res. Commun. 189:1747-1753(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryonic stem cell.
[4]"Tie2, a putative protein tyrosine kinase from a new class of cell surface receptor."
Runting A.S., Stacker S.A., Wilks A.F.
Growth Factors 9:99-105(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[5]"Expression of tie-2, a member of a novel family of receptor tyrosine kinases, in the endothelial cell lineage."
Schnuerch H., Risau W.
Development 119:957-968(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Molecular cloning and characterization of mouse TIE and TEK receptor tyrosine kinase genes and their expression in hematopoietic stem cells."
Iwama A., Hamaguchi I., Hashiyama M., Murayama Y., Yasunaga K., Suda T.
Biochem. Biophys. Res. Commun. 195:301-309(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Hematopoietic stem cell.
[7]"Tek, a novel tyrosine kinase gene located on mouse chromosome 4, is expressed in endothelial cells and their presumptive precursors."
Dumont D.J., Yamaguchi T.P., Conlon R.A., Rossant J., Breitman M.L.
Oncogene 7:1471-1480(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 822-1122.
Strain: CD-1.
Tissue: Embryonic heart.
[8]"Dominant-negative and targeted null mutations in the endothelial receptor tyrosine kinase, tek, reveal a critical role in vasculogenesis of the embryo."
Dumont D.J., Gradwohl G., Fong G.H., Puri M.C., Gertsenstein M., Auerbach A., Breitman M.L.
Genes Dev. 8:1897-1909(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-853, CATALYTIC ACTIVITY, FUNCTION.
[9]"Distinct roles of the receptor tyrosine kinases Tie-1 and Tie-2 in blood vessel formation."
Sato T.N., Tozawa Y., Deutsch U., Wolburg-Buchholz K., Fujiwara Y., Gendron-Maguire M., Gridley T., Wolburg H., Risau W., Qin Y.
Nature 376:70-74(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[10]"Tyrosine 1101 of Tie2 is the major site of association of p85 and is required for activation of phosphatidylinositol 3-kinase and Akt."
Kontos C.D., Stauffer T.P., Yang W.P., York J.D., Huang L., Blanar M.A., Meyer T., Peters K.G.
Mol. Cell. Biol. 18:4131-4140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIK3R1, MUTAGENESIS OF TYR-1100, FUNCTION IN ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE AND AKT1.
[11]"Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration."
Jones N., Master Z., Jones J., Bouchard D., Gunji Y., Sasaki H., Daly R., Alitalo K., Dumont D.J.
J. Biol. Chem. 274:30896-30905(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB2; GRB7, GRB14, PTPN11/SHP2 AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF GRB7 AND PIK3R1, MUTAGENESIS OF TYR-1100.
[12]"Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2."
Fachinger G., Deutsch U., Risau W.
Oncogene 18:5948-5953(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRB.
[13]"Rescue of the early vascular defects in Tek/Tie2 null mice reveals an essential survival function."
Jones N., Voskas D., Master Z., Sarao R., Jones J., Dumont D.J.
EMBO Rep. 2:438-445(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ANTI-APOPTOTIC FUNCTION.
[14]"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."
Fiedler U., Krissl T., Koidl S., Weiss C., Koblizek T., Deutsch U., Martiny-Baron G., Marme D., Augustin H.G.
J. Biol. Chem. 278:1721-1727(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANGPT1 AND ANGPT2, DOMAIN.
[15]"A unique autophosphorylation site on Tie2/Tek mediates Dok-R phosphotyrosine binding domain binding and function."
Jones N., Chen S.H., Sturk C., Master Z., Tran J., Kerbel R.S., Dumont D.J.
Mol. Cell. Biol. 23:2658-2668(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1100 AND TYR-1106, MUTAGENESIS OF LYS-853; TYR-1100 AND TYR-1106, FUNCTION IN DOK2 PHOSPHORYLATION, INTERACTION WITH DOK2.
[16]"Biological characterization of angiopoietin-3 and angiopoietin-4."
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.
FASEB J. 18:1200-1208(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS ANGPT4 RECEPTOR AND IN ACTIVATION OF AKT1, INTERACTION WITH ANGPT4, AUTOPHOSPHORYLATION.
[17]"VE-PTP controls blood vessel development by balancing Tie-2 activity."
Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F., Deutsch U., Nottebaum A.F., Vestweber D.
J. Cell Biol. 185:657-671(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPRB.
[18]"Tyrosine phosphorylation of Grb14 by Tie2."
Sturk C., Dumont D.J.
Cell Commun. Signal. 8:30-30(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB14, FUNCTION IN GRB14 PHOSPHORYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71426 mRNA. Translation: CAA50557.1.
X67553 mRNA. Translation: CAA47857.1.
D13738 mRNA. Translation: BAA02883.1.
S67051 mRNA. Translation: AAB28663.1.
PIRI54237.
JH0771.
JN0712.
RefSeqXP_006502992.1. XM_006502929.1.
UniGeneMm.14313.

3D structure databases

ProteinModelPortalQ02858.
SMRQ02858. Positions 23-534, 811-1119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6050N.
IntActQ02858. 7 interactions.
MINTMINT-4137861.

Chemistry

BindingDBQ02858.
ChEMBLCHEMBL5199.

PTM databases

PhosphoSiteQ02858.

Proteomic databases

PaxDbQ02858.
PRIDEQ02858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071168; ENSMUSP00000071162; ENSMUSG00000006386.
GeneID21687.
UCSCuc008tsk.1. mouse.

Organism-specific databases

MGIMGI:98664. Tek.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117500.
HOGENOMHOG000049232.
HOVERGENHBG007316.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressQ02858.
BgeeQ02858.
CleanExMM_TEK.
GenevestigatorQ02858.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR018941. Tyr_kin_Tie2_Ig-like_dom-1_N.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF00041. fn3. 3 hits.
PF10430. Ig_Tie2_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00181. EGF. 1 hit.
SM00180. EGF_Lam. 1 hit.
SM00060. FN3. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEPS00022. EGF_1. 3 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 1 hit.
PS50853. FN3. 3 hits.
PS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ02858.
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Entry information

Entry nameTIE2_MOUSE
AccessionPrimary (citable) accession number: Q02858
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot