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Q02858

- TIE2_MOUSE

UniProt

Q02858 - TIE2_MOUSE

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Protein

Angiopoietin-1 receptor

Gene

Tek

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 TIE1.7 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei853 – 8531ATPPROSITE-ProRule annotation
Active sitei962 – 9621Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi828 – 8369ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein tyrosine kinase activity Source: UniProtKB
  3. receptor activity Source: MGI
  4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. cell-matrix adhesion Source: MGI
  3. endothelial cell proliferation Source: UniProtKB
  4. heart development Source: UniProtKB
  5. heart trabecula formation Source: UniProtKB
  6. hemopoiesis Source: MGI
  7. negative regulation of angiogenesis Source: UniProtKB
  8. negative regulation of apoptotic process Source: MGI
  9. negative regulation of endothelial cell apoptotic process Source: UniProtKB
  10. patterning of blood vessels Source: DFLAT
  11. peptidyl-tyrosine phosphorylation Source: UniProtKB
  12. positive regulation of angiogenesis Source: UniProtKB
  13. positive regulation of cell adhesion Source: MGI
  14. positive regulation of endothelial cell migration Source: UniProtKB
  15. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  16. positive regulation of focal adhesion assembly Source: UniProtKB
  17. positive regulation of intracellular signal transduction Source: UniProtKB
  18. positive regulation of peptidyl-serine phosphorylation Source: MGI
  19. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  20. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  21. positive regulation of protein kinase B signaling Source: UniProtKB
  22. positive regulation of protein phosphorylation Source: UniProtKB
  23. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: DFLAT
  24. protein autophosphorylation Source: UniProtKB
  25. regulation of angiogenesis Source: MGI
  26. regulation of cell migration Source: MGI
  27. regulation of endothelial cell proliferation Source: DFLAT
  28. regulation of establishment or maintenance of cell polarity Source: UniProtKB
  29. response to retinoic acid Source: BHF-UCL
  30. single organismal cell-cell adhesion Source: MGI
  31. sprouting angiogenesis Source: UniProtKB
  32. substrate adhesion-dependent cell spreading Source: UniProtKB
  33. Tie signaling pathway Source: UniProtKB
  34. transmembrane receptor protein tyrosine kinase signaling pathway Source: UniProtKB
  35. vasculogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_211860. Tie2 Signaling.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Tek
Synonyms:Hyk, Tie-2, Tie2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:98664. Tek.

Subcellular locationi

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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 746724ExtracellularSequence AnalysisAdd
BLAST
Transmembranei747 – 76721HelicalSequence AnalysisAdd
BLAST
Topological domaini768 – 1122355CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. extracellular region Source: UniProtKB-KW
  5. integral component of membrane Source: MGI
  6. integral component of plasma membrane Source: InterPro
  7. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi853 – 8531K → A: Loss of kinase activity. 2 Publications
Mutagenesisi1100 – 11001Y → F: Reduced levels of autophosphorylation. Abolishes interaction with GRB2 and GRB7. Abolishes phosphorylation of GRB7 and PIK3R1. 3 Publications
Mutagenesisi1106 – 11061Y → F: Reduced levels of autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222By similarityAdd
BLAST
Chaini23 – 11221100Angiopoietin-1 receptorPRO_0000024475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 102By similarity
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi211 ↔ 220By similarity
Disulfide bondi224 ↔ 233By similarity
Disulfide bondi227 ↔ 240By similarity
Disulfide bondi242 ↔ 251By similarity
Disulfide bondi255 ↔ 264By similarity
Disulfide bondi268 ↔ 274By similarity
Disulfide bondi280 ↔ 287By similarity
Disulfide bondi289 ↔ 298By similarity
Disulfide bondi302 ↔ 311By similarity
Disulfide bondi315 ↔ 323By similarity
Disulfide bondi317 ↔ 329By similarity
Disulfide bondi331 ↔ 340By similarity
Disulfide bondi370 ↔ 424By similarity
Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi558 – 5581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi595 – 5951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi648 – 6481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis
Modified residuei858 – 8581Phosphotyrosine; by autocatalysisBy similarity
Modified residuei990 – 9901Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1100 – 11001Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1106 – 11061Phosphotyrosine; by autocatalysis1 Publication

Post-translational modificationi

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.By similarity2 Publications
Ubiquitinated. The phosphorylated receptor is ubiquitinated and internalized, leading to its degradation (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ02858.
PRIDEiQ02858.

PTM databases

PhosphoSiteiQ02858.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Expression detectable in day 8.5 embryos.

Gene expression databases

BgeeiQ02858.
CleanExiMM_TEK.
ExpressionAtlasiQ02858. baseline and differential.
GenevestigatoriQ02858.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Grb2Q606313EBI-7099626,EBI-1688
Grb7Q031603EBI-7099626,EBI-7100053

Protein-protein interaction databases

DIPiDIP-6050N.
IntActiQ02858. 7 interactions.
MINTiMINT-4137861.

Structurei

3D structure databases

ProteinModelPortaliQ02858.
SMRiQ02858. Positions 23-534, 811-1119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 12380Ig-like C2-type 1Add
BLAST
Domaini210 – 25243EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini254 – 29946EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini301 – 34141EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini350 – 44091Ig-like C2-type 2Add
BLAST
Domaini444 – 53996Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini543 – 63593Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini640 – 73394Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini822 – 1094273Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily.PROSITE-ProRule annotation
Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120533.
HOGENOMiHOG000049232.
HOVERGENiHBG007316.
InParanoidiQ02858.
KOiK05121.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR000742. 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]
PfamiPF00041. fn3. 3 hits.
PF10430. Ig_Tie2_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00181. EGF. 1 hit.
SM00180. EGF_Lam. 1 hit.
SM00060. FN3. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00022. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q02858-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSLAGLVLC GVSLLLYGVV EGAMDLILIN SLPLVSDAET SLTCIASGWH
60 70 80 90 100
PHEPITIGRD FEALMNQHQD PLEVTQDVTR EWAKKVVWKR EKASKINGAY
110 120 130 140 150
FCEGRVRGQA IRIRTMKMRQ QASFLPATLT MTVDRGDNVN ISFKKVLIKE
160 170 180 190 200
EDAVIYKNGS FIHSVPRHEV PDILEVHLPH AQPQDAGVYS ARYIGGNLFT
210 220 230 240 250
SAFTRLIVRR CEAQKWGPDC SRPCTTCKNN GVCHEDTGEC ICPPGFMGRT
260 270 280 290 300
CEKACEPHTF GRTCKERCSG PEGCKSYVFC LPDPYGCSCA TGWRGLQCNE
310 320 330 340 350
ACPSGYYGPD CKLRCHCTNE EICDRFQGCL CSQGWQGLQC EKEGRPRMTP
360 370 380 390 400
QIEDLPDHIE VNSGKFNPIC KASGWPLPTS EEMTLVKPDG TVLQPNDFNY
410 420 430 440 450
TDRFSVAIFT VNRVLPPDSG VWVCSVNTVA GMVEKPFNIS VKVLPEPLHA
460 470 480 490 500
PNVIDTGHNF AIINISSEPY FGDGPIKSKK LFYKPVNQAW KYIEVTNEIF
510 520 530 540 550
TLNYLEPRTD YELCVQLARP GEGGEGHPGP VRRFTTASIG LPPPRGLSLL
560 570 580 590 600
PKSQTALNLT WQPIFTNSED EFYVEVERRS LQTTSDQQNI KVPGNLTSVL
610 620 630 640 650
LSNLVPREQY TVRARVNTKA QGEWSEELRA WTLSDILPPQ PENIKISNIT
660 670 680 690 700
DSTAMVSWTI VDGYSISSII IRYKVQGKNE DQHIDVKIKN ATVTQYQLKG
710 720 730 740 750
LEPETTYHVD IFAENNIGSS NPAFSHELRT LPHSPASADL GGGKMLLIAI
760 770 780 790 800
LGSAGMTCIT VLLAFLIMLQ LKRANVQRRM AQAFQNREEP AVQFNSGTLA
810 820 830 840 850
LNRKAKNNPD PTIYPVLDWN DIKFQDVIGE GNFGQVLKAR IKKDGLRMDA
860 870 880 890 900
AIKRMKEYAS KDDHRDFAGE LEVLCKLGHH PNIINLLGAC EHRGYLYLAI
910 920 930 940 950
EYAPHGNLLD FLRKSRVLET DPAFAIANST ASTLSSQQLL HFAADVARGM
960 970 980 990 1000
DYLSQKQFIH RDLAARNILV GENYIAKIAD FGLSRGQEVY VKKTMGRLPV
1010 1020 1030 1040 1050
RWMAIESLNY SVYTTNSDVW SYGVLLWEIV SLGGTPYCGM TCAELYEKLP
1060 1070 1080 1090 1100
QGYRLEKPLN CDDEVYDLMR QCWREKPYER PSFAQILVSL NRMLEERKTY
1110 1120
VNTTLYEKFT YAGIDCSAEE AA
Length:1,122
Mass (Da):125,701
Last modified:February 1, 1995 - v2
Checksum:iF879623D103FFE96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 17111FIHSVPRHEVP → LHPLSAPGMKYL in BAA02883. (PubMed:1282811)CuratedAdd
BLAST
Sequence conflicti538 – 5381S → C in CAA47857. (PubMed:8386827)Curated
Sequence conflicti736 – 7361A → G in CAA47857. (PubMed:8386827)Curated
Sequence conflicti736 – 7361A → G in AAB28663. (PubMed:8217221)Curated
Sequence conflicti745 – 76117MLLIA…TCITV → DATHSHPWVWNDFASPC in BAA02883. (PubMed:1282811)CuratedAdd
BLAST
Sequence conflicti786 – 7861N → NV in BAA02883. (PubMed:1282811)Curated
Sequence conflicti786 – 7861N → NV no nucleotide entry (PubMed:8395828)Curated
Sequence conflicti913 – 9131R → G in BAA02883. (PubMed:1282811)Curated
Sequence conflicti925 – 9317AIANSTA → CHRQQYS in BAA02883. (PubMed:1282811)Curated
Sequence conflicti1117 – 11171S → P in BAA02883. (PubMed:1282811)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71426 mRNA. Translation: CAA50557.1.
X67553 mRNA. Translation: CAA47857.1.
D13738 mRNA. Translation: BAA02883.1.
S67051 mRNA. Translation: AAB28663.1.
CCDSiCCDS71421.1.
PIRiI54237.
JH0771.
JN0712.
RefSeqiNP_001277478.1. NM_001290549.1.
UniGeneiMm.14313.

Genome annotation databases

EnsembliENSMUST00000071168; ENSMUSP00000071162; ENSMUSG00000006386.
GeneIDi21687.
KEGGimmu:21687.
UCSCiuc008tsk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71426 mRNA. Translation: CAA50557.1 .
X67553 mRNA. Translation: CAA47857.1 .
D13738 mRNA. Translation: BAA02883.1 .
S67051 mRNA. Translation: AAB28663.1 .
CCDSi CCDS71421.1.
PIRi I54237.
JH0771.
JN0712.
RefSeqi NP_001277478.1. NM_001290549.1.
UniGenei Mm.14313.

3D structure databases

ProteinModelPortali Q02858.
SMRi Q02858. Positions 23-534, 811-1119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6050N.
IntActi Q02858. 7 interactions.
MINTi MINT-4137861.

Chemistry

BindingDBi Q02858.
ChEMBLi CHEMBL5199.

PTM databases

PhosphoSitei Q02858.

Proteomic databases

PaxDbi Q02858.
PRIDEi Q02858.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071168 ; ENSMUSP00000071162 ; ENSMUSG00000006386 .
GeneIDi 21687.
KEGGi mmu:21687.
UCSCi uc008tsk.1. mouse.

Organism-specific databases

CTDi 7010.
MGIi MGI:98664. Tek.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120533.
HOGENOMi HOG000049232.
HOVERGENi HBG007316.
InParanoidi Q02858.
KOi K05121.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_211860. Tie2 Signaling.

Miscellaneous databases

PROi Q02858.
SOURCEi Search...

Gene expression databases

Bgeei Q02858.
CleanExi MM_TEK.
ExpressionAtlasi Q02858. baseline and differential.
Genevestigatori Q02858.

Family and domain databases

Gene3Di 2.60.40.10. 5 hits.
InterProi IPR000742. 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 ]
Pfami PF00041. fn3. 3 hits.
PF10430. Ig_Tie2_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR00109. TYRKINASE.
SMARTi SM00181. EGF. 1 hit.
SM00180. EGF_Lam. 1 hit.
SM00060. FN3. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00022. 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 ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiTIE2_MOUSE
AccessioniPrimary (citable) accession number: Q02858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3