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Entry version 210 (08 May 2019)
Sequence version 2 (16 Dec 2008)
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Protein

Angiopoietin-1 receptor

Gene

TEK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 TIE1.10 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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.6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei855ATPCurated1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei964Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi830 – 838ATPCurated9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processAngiogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-210993 Tie2 Signaling
R-HSA-5673001 RAF/MAP kinase cascade

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q02763

SIGNOR Signaling Network Open Resource

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SIGNORi
Q02763

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Angiopoietin-1 receptor (EC:2.7.10.1)
Alternative name(s):
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
Short name:
hTIE2
p140 TEK
CD_antigen: CD202b
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TEK
Synonyms:TIE2, VMCM, VMCM1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:11724 TEK

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600221 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q02763

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini23 – 748ExtracellularSequence analysisAdd BLAST726
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei749 – 769HelicalSequence analysisAdd BLAST21
Topological domaini770 – 1124CytoplasmicSequence analysisAdd BLAST355

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Dominantly inherited venous malformations (VMCM)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn error of vascular morphogenesis characterized by dilated, serpiginous channels.
See also OMIM:600195
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_006352849R → W in VMCM; increased ligand-independent autophosphorylation and kinase activation; no effect on location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs80338908EnsemblClinVar.1
Natural variantiVAR_066606897Y → C in VMCM; increased ligand-independent autophosphorylation and kinase activation. 1 PublicationCorresponds to variant dbSNP:rs80338909EnsemblClinVar.1
Natural variantiVAR_008716897Y → S in VMCM; also found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation and kinase activation. 3 PublicationsCorresponds to variant dbSNP:rs80338909EnsemblClinVar.1
Natural variantiVAR_066607915R → H in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation. 1 PublicationCorresponds to variant dbSNP:rs387906745EnsemblClinVar.1
Natural variantiVAR_066608918R → C in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Natural variantiVAR_066609919V → L in VMCM; increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Natural variantiVAR_066610925A → S in VMCM; increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Natural variantiVAR_0666111100K → N in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Somatic mutations of TEK are associated with solitary and multiple sporadic venous malformations.1 Publication
May play a role in a range of diseases with a vascular component, including neovascularization of tumors, psoriasis and inflammation.
Glaucoma 3, primary congenital, E (GLC3E)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:617272
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07804519 – 210Missing in GLC3E; formation of protein aggregates. 1 PublicationAdd BLAST192
Natural variantiVAR_078046233C → Y in GLC3E; enhanced proteasomal degradation. 1 Publication1
Natural variantiVAR_078047294K → N in GLC3E; unknown pathological significance; 10-fold decrease of Tyr-1102 phosphorylation; no effect on membrane location. 1 PublicationCorresponds to variant dbSNP:rs146169480Ensembl.1
Natural variantiVAR_078048611Y → C in GLC3E; reduced response to ligand; loss of ligand-induced phosphorylation; no effect on basal membrane location. 1 PublicationCorresponds to variant dbSNP:rs1306527531Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi224C → S: Reduces protein abundance. 1 Publication1
Mutagenesisi855K → R: Loss of kinase activity. 2 Publications1
Mutagenesisi1102Y → F: Abolishes interaction with SHC1. 1 Publication1

Keywords - Diseasei

Disease mutation, Glaucoma

Organism-specific databases

DisGeNET

More...
DisGeNETi
7010

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
TEK

MalaCards human disease database

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MalaCardsi
TEK
MIMi600195 phenotype
617272 phenotype

Open Targets

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OpenTargetsi
ENSG00000120156

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
1059 Blue rubber bleb nevus
98976 Congenital glaucoma
2451 Mucocutaneous venous malformations

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36441

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4128

Drug and drug target database

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DrugBanki
DB00415 Ampicillin
DB08221 N-{4-METHYL-3-[(3-PYRIMIDIN-4-YLPYRIDIN-2-YL)AMINO]PHENYL}-3-(TRIFLUOROMETHYL)BENZAMIDE
DB08901 Ponatinib
DB08896 Regorafenib
DB05294 Vandetanib
DB05153 XL184

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1842

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TEK

Domain mapping of disease mutations (DMDM)

More...
DMDMi
218511853

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 221 PublicationAdd BLAST22
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002447423 – 1124Angiopoietin-1 receptorAdd BLAST1102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi44 ↔ 1021 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi140N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi158N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi211 ↔ 2201 Publication
Disulfide bondi224 ↔ 2331 Publication
Disulfide bondi227 ↔ 2401 Publication
Disulfide bondi242 ↔ 2511 Publication
Disulfide bondi255 ↔ 2641 Publication
Disulfide bondi268 ↔ 2741 Publication
Disulfide bondi280 ↔ 2871 Publication
Disulfide bondi289 ↔ 2981 Publication
Disulfide bondi302 ↔ 3111 Publication
Disulfide bondi315 ↔ 3231 Publication
Disulfide bondi317 ↔ 3291 Publication
Disulfide bondi331 ↔ 3401 Publication
Disulfide bondi370 ↔ 4241 Publication
Glycosylationi399N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi438N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi464N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi560N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi596N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi649N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi691N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei860Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei992Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1102Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1108Phosphotyrosine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytic processing leads to the shedding of the extracellular domain (soluble TIE-2 alias sTIE-2).1 Publication
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.2 Publications
Ubiquitinated. The phosphorylated receptor is ubiquitinated and internalized, leading to its degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q02763

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q02763

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q02763

PeptideAtlas

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PeptideAtlasi
Q02763

PRoteomics IDEntifications database

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PRIDEi
Q02763

ProteomicsDB human proteome resource

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ProteomicsDBi
58121
58122 [Q02763-2]
58123 [Q02763-3]

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
769

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q02763

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q02763

UniCarbKB; an annotated and curated database of glycan structures

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UniCarbKBi
Q02763

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000120156 Expressed in 192 organ(s), highest expression level in metanephric glomerulus

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q02763 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q02763 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB010359
HPA073265

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 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).13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112869, 19 interactors

Database of interacting proteins

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DIPi
DIP-6047N

Protein interaction database and analysis system

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IntActi
Q02763, 22 interactors

Molecular INTeraction database

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MINTi
Q02763

STRING: functional protein association networks

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STRINGi
9606.ENSP00000369375

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q02763

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FVRX-ray2.20A/B808-1124[»]
2GY5X-ray2.90A23-445[»]
2GY7X-ray3.70B23-445[»]
2OO8X-ray2.20X808-1124[»]
2OSCX-ray2.80A808-1124[»]
2P4IX-ray2.50A/B808-1124[»]
2WQBX-ray2.95A802-1124[»]
3BEAX-ray2.02A917-935[»]
3L8PX-ray2.40A808-1124[»]
4K0VX-ray4.51A23-542[»]
4X3JX-ray2.50A802-1122[»]
5MYAX-ray2.90A/B443-742[»]
5MYBX-ray2.60A/B443-742[»]
5UTKX-ray2.50A/B442-741[»]
6MWEX-ray2.05A/B808-1124[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q02763

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q02763

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini44 – 123Ig-like C2-type 1Add BLAST80
Domaini210 – 252EGF-like 1PROSITE-ProRule annotationAdd BLAST43
Domaini254 – 299EGF-like 2PROSITE-ProRule annotationAdd BLAST46
Domaini301 – 341EGF-like 3PROSITE-ProRule annotationAdd BLAST41
Domaini350 – 440Ig-like C2-type 2Add BLAST91
Domaini447 – 541Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST95
Domaini545 – 636Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST92
Domaini641 – 735Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST95
Domaini824 – 1096Protein kinasePROSITE-ProRule annotationAdd BLAST273

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Tie subfamily.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158840

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000049232

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q02763

KEGG Orthology (KO)

More...
KOi
K05121

Identification of Orthologs from Complete Genome Data

More...
OMAi
CEKEGMP

Database of Orthologous Groups

More...
OrthoDBi
1040796at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q02763

TreeFam database of animal gene trees

More...
TreeFami
TF317568

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00063 FN3, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 6 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR011009 Kinase-like_dom_sf
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00041 fn3, 3 hits
PF10430 Ig_Tie2_1, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181 EGF, 3 hits
SM00060 FN3, 3 hits
SM00220 S_TKc, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 1 hit
SSF49265 SSF49265, 2 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q02763-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MDSLASLVLC GVSLLLSGTV EGAMDLILIN SLPLVSDAET SLTCIASGWR
60 70 80 90 100
PHEPITIGRD FEALMNQHQD PLEVTQDVTR EWAKKVVWKR EKASKINGAY
110 120 130 140 150
FCEGRVRGEA IRIRTMKMRQ QASFLPATLT MTVDKGDNVN ISFKKVLIKE
160 170 180 190 200
EDAVIYKNGS FIHSVPRHEV PDILEVHLPH AQPQDAGVYS ARYIGGNLFT
210 220 230 240 250
SAFTRLIVRR CEAQKWGPEC NHLCTACMNN GVCHEDTGEC ICPPGFMGRT
260 270 280 290 300
CEKACELHTF GRTCKERCSG QEGCKSYVFC LPDPYGCSCA TGWKGLQCNE
310 320 330 340 350
ACHPGFYGPD CKLRCSCNNG EMCDRFQGCL CSPGWQGLQC EREGIQRMTP
360 370 380 390 400
KIVDLPDHIE VNSGKFNPIC KASGWPLPTN EEMTLVKPDG TVLHPKDFNH
410 420 430 440 450
TDHFSVAIFT IHRILPPDSG VWVCSVNTVA GMVEKPFNIS VKVLPKPLNA
460 470 480 490 500
PNVIDTGHNF AVINISSEPY FGDGPIKSKK LLYKPVNHYE AWQHIQVTNE
510 520 530 540 550
IVTLNYLEPR TEYELCVQLV RRGEGGEGHP GPVRRFTTAS IGLPPPRGLN
560 570 580 590 600
LLPKSQTTLN LTWQPIFPSS EDDFYVEVER RSVQKSDQQN IKVPGNLTSV
610 620 630 640 650
LLNNLHPREQ YVVRARVNTK AQGEWSEDLT AWTLSDILPP QPENIKISNI
660 670 680 690 700
THSSAVISWT ILDGYSISSI TIRYKVQGKN EDQHVDVKIK NATITQYQLK
710 720 730 740 750
GLEPETAYQV DIFAENNIGS SNPAFSHELV TLPESQAPAD LGGGKMLLIA
760 770 780 790 800
ILGSAGMTCL TVLLAFLIIL QLKRANVQRR MAQAFQNVRE EPAVQFNSGT
810 820 830 840 850
LALNRKVKNN PDPTIYPVLD WNDIKFQDVI GEGNFGQVLK ARIKKDGLRM
860 870 880 890 900
DAAIKRMKEY ASKDDHRDFA GELEVLCKLG HHPNIINLLG ACEHRGYLYL
910 920 930 940 950
AIEYAPHGNL LDFLRKSRVL ETDPAFAIAN STASTLSSQQ LLHFAADVAR
960 970 980 990 1000
GMDYLSQKQF IHRDLAARNI LVGENYVAKI ADFGLSRGQE VYVKKTMGRL
1010 1020 1030 1040 1050
PVRWMAIESL NYSVYTTNSD VWSYGVLLWE IVSLGGTPYC GMTCAELYEK
1060 1070 1080 1090 1100
LPQGYRLEKP LNCDDEVYDL MRQCWREKPY ERPSFAQILV SLNRMLEERK
1110 1120
TYVNTTLYEK FTYAGIDCSA EEAA
Length:1,124
Mass (Da):125,830
Last modified:December 16, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE739DEC3E4FEB124
GO
Isoform 2 (identifier: Q02763-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     300-342: Missing.

Show »
Length:1,081
Mass (Da):121,048
Checksum:iFA9BF050B49AB557
GO
Isoform 3 (identifier: Q02763-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     18-121: Missing.
     300-342: Missing.
     788-788: Missing.

Show »
Length:976
Mass (Da):109,141
Checksum:iCE8D06A4F93D48E0
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B5A954B5A954_HUMAN
Angiopoietin-1 receptor
TEK
468Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RIV9E5RIV9_HUMAN
Angiopoietin-1 receptor
TEK
468Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti536F → L in BAG58094 (PubMed:14702039).Curated1
Sequence conflicti695T → I in AAA61139 (PubMed:8382358).Curated1
Sequence conflicti939 – 940QQ → HH in AAH35514 (PubMed:15489334).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07804519 – 210Missing in GLC3E; formation of protein aggregates. 1 PublicationAdd BLAST192
Natural variantiVAR_035714117K → N in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. 2 Publications1
Natural variantiVAR_041855148I → T1 PublicationCorresponds to variant dbSNP:rs35969327EnsemblClinVar.1
Natural variantiVAR_041856226A → V1 PublicationCorresponds to variant dbSNP:rs35814893EnsemblClinVar.1
Natural variantiVAR_078046233C → Y in GLC3E; enhanced proteasomal degradation. 1 Publication1
Natural variantiVAR_078047294K → N in GLC3E; unknown pathological significance; 10-fold decrease of Tyr-1102 phosphorylation; no effect on membrane location. 1 PublicationCorresponds to variant dbSNP:rs146169480Ensembl.1
Natural variantiVAR_048002346Q → P4 PublicationsCorresponds to variant dbSNP:rs682632Ensembl.1
Natural variantiVAR_048003391T → I. Corresponds to variant dbSNP:rs34032300EnsemblClinVar.1
Natural variantiVAR_024578486V → I1 PublicationCorresponds to variant dbSNP:rs1334811EnsemblClinVar.1
Natural variantiVAR_041857600V → L1 PublicationCorresponds to variant dbSNP:rs35030851EnsemblClinVar.1
Natural variantiVAR_078048611Y → C in GLC3E; reduced response to ligand; loss of ligand-induced phosphorylation; no effect on basal membrane location. 1 PublicationCorresponds to variant dbSNP:rs1306527531Ensembl.1
Natural variantiVAR_041858634L → F1 PublicationCorresponds to variant dbSNP:rs35378598EnsemblClinVar.1
Natural variantiVAR_041859676V → I1 PublicationCorresponds to variant dbSNP:rs56367117Ensembl.1
Natural variantiVAR_041860724A → T1 PublicationCorresponds to variant dbSNP:rs4631561EnsemblClinVar.1
Natural variantiVAR_006352849R → W in VMCM; increased ligand-independent autophosphorylation and kinase activation; no effect on location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs80338908EnsemblClinVar.1
Natural variantiVAR_041861883P → A in an ovarian serous carcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1490428165Ensembl.1
Natural variantiVAR_066606897Y → C in VMCM; increased ligand-independent autophosphorylation and kinase activation. 1 PublicationCorresponds to variant dbSNP:rs80338909EnsemblClinVar.1
Natural variantiVAR_078049897Y → F Found in a patient with multiple sporadic venous malformations; increased ligand-independent autophosphorylation; the hyperphosphorylation increases when associated with Leu-915. 1 Publication1
Natural variantiVAR_078050897Y → H Found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation. 1 Publication1
Natural variantiVAR_008716897Y → S in VMCM; also found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation and kinase activation. 3 PublicationsCorresponds to variant dbSNP:rs80338909EnsemblClinVar.1
Natural variantiVAR_078051914L → 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. 1 Publication1
Natural variantiVAR_078052915R → C Found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation. 1 Publication1
Natural variantiVAR_066607915R → H in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation. 1 PublicationCorresponds to variant dbSNP:rs387906745EnsemblClinVar.1
Natural variantiVAR_078053915R → L Found in a patient with multiple sporadic venous malformations; increased ligand-independent autophosphorylation; the autophosphorylation increases when associated with Phe-897. 1 Publication1
Natural variantiVAR_078054917S → I Found in a patient with solitary sporadic venous malformations; increased ligand-independent autophosphorylation. 1 Publication1
Natural variantiVAR_066608918R → C in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Natural variantiVAR_066609919V → L in VMCM; increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Natural variantiVAR_066610925A → S in VMCM; increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Natural variantiVAR_0666111100K → N in VMCM; strongly increased ligand-independent autophosphorylation and kinase activation. 1 Publication1
Natural variantiVAR_0418621124A → V in a renal clear cell carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_04213718 – 121Missing in isoform 3. 1 PublicationAdd BLAST104
Alternative sequenceiVSP_042138300 – 342Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST43
Alternative sequenceiVSP_042139788Missing in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L06139 mRNA Translation: AAA61139.1
AK291775 mRNA Translation: BAF84464.1
AK294887 mRNA Translation: BAG57981.1
AK295043 mRNA Translation: BAG58094.1
AL133411 Genomic DNA No translation available.
AL355432 Genomic DNA No translation available.
AL355433 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58571.1
CH471071 Genomic DNA Translation: EAW58572.1
BC035514 mRNA Translation: AAH35514.2

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6519.1 [Q02763-1]
CCDS75825.1 [Q02763-2]
CCDS78389.1 [Q02763-3]

Protein sequence database of the Protein Information Resource

More...
PIRi
I58388

NCBI Reference Sequences

More...
RefSeqi
NP_000450.2, NM_000459.4
NP_001277006.1, NM_001290077.1
NP_001277007.1, NM_001290078.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000380036; ENSP00000369375; ENSG00000120156 [Q02763-1]
ENST00000406359; ENSP00000383977; ENSG00000120156 [Q02763-2]
ENST00000519097; ENSP00000430686; ENSG00000120156 [Q02763-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7010

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7010

UCSC genome browser

More...
UCSCi
uc003zqi.5 human [Q02763-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06139 mRNA Translation: AAA61139.1
AK291775 mRNA Translation: BAF84464.1
AK294887 mRNA Translation: BAG57981.1
AK295043 mRNA Translation: BAG58094.1
AL133411 Genomic DNA No translation available.
AL355432 Genomic DNA No translation available.
AL355433 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58571.1
CH471071 Genomic DNA Translation: EAW58572.1
BC035514 mRNA Translation: AAH35514.2
CCDSiCCDS6519.1 [Q02763-1]
CCDS75825.1 [Q02763-2]
CCDS78389.1 [Q02763-3]
PIRiI58388
RefSeqiNP_000450.2, NM_000459.4
NP_001277006.1, NM_001290077.1
NP_001277007.1, NM_001290078.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FVRX-ray2.20A/B808-1124[»]
2GY5X-ray2.90A23-445[»]
2GY7X-ray3.70B23-445[»]
2OO8X-ray2.20X808-1124[»]
2OSCX-ray2.80A808-1124[»]
2P4IX-ray2.50A/B808-1124[»]
2WQBX-ray2.95A802-1124[»]
3BEAX-ray2.02A917-935[»]
3L8PX-ray2.40A808-1124[»]
4K0VX-ray4.51A23-542[»]
4X3JX-ray2.50A802-1122[»]
5MYAX-ray2.90A/B443-742[»]
5MYBX-ray2.60A/B443-742[»]
5UTKX-ray2.50A/B442-741[»]
6MWEX-ray2.05A/B808-1124[»]
SMRiQ02763
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112869, 19 interactors
DIPiDIP-6047N
IntActiQ02763, 22 interactors
MINTiQ02763
STRINGi9606.ENSP00000369375

Chemistry databases

BindingDBiQ02763
ChEMBLiCHEMBL4128
DrugBankiDB00415 Ampicillin
DB08221 N-{4-METHYL-3-[(3-PYRIMIDIN-4-YLPYRIDIN-2-YL)AMINO]PHENYL}-3-(TRIFLUOROMETHYL)BENZAMIDE
DB08901 Ponatinib
DB08896 Regorafenib
DB05294 Vandetanib
DB05153 XL184
GuidetoPHARMACOLOGYi1842

PTM databases

GlyConnecti769
iPTMnetiQ02763
PhosphoSitePlusiQ02763
UniCarbKBiQ02763

Polymorphism and mutation databases

BioMutaiTEK
DMDMi218511853

Proteomic databases

EPDiQ02763
jPOSTiQ02763
PaxDbiQ02763
PeptideAtlasiQ02763
PRIDEiQ02763
ProteomicsDBi58121
58122 [Q02763-2]
58123 [Q02763-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7010
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380036; ENSP00000369375; ENSG00000120156 [Q02763-1]
ENST00000406359; ENSP00000383977; ENSG00000120156 [Q02763-2]
ENST00000519097; ENSP00000430686; ENSG00000120156 [Q02763-3]
GeneIDi7010
KEGGihsa:7010
UCSCiuc003zqi.5 human [Q02763-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7010
DisGeNETi7010

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TEK
GeneReviewsiTEK
HGNCiHGNC:11724 TEK
HPAiCAB010359
HPA073265
MalaCardsiTEK
MIMi600195 phenotype
600221 gene
617272 phenotype
neXtProtiNX_Q02763
OpenTargetsiENSG00000120156
Orphaneti1059 Blue rubber bleb nevus
98976 Congenital glaucoma
2451 Mucocutaneous venous malformations
PharmGKBiPA36441

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158840
HOGENOMiHOG000049232
InParanoidiQ02763
KOiK05121
OMAiCEKEGMP
OrthoDBi1040796at2759
PhylomeDBiQ02763
TreeFamiTF317568

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-210993 Tie2 Signaling
R-HSA-5673001 RAF/MAP kinase cascade
SignaLinkiQ02763
SIGNORiQ02763

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
TEK human
EvolutionaryTraceiQ02763

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TEK_tyrosine_kinase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
7010

Protein Ontology

More...
PROi
PR:Q02763

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000120156 Expressed in 192 organ(s), highest expression level in metanephric glomerulus
ExpressionAtlasiQ02763 baseline and differential
GenevisibleiQ02763 HS

Family and domain databases

CDDicd00063 FN3, 2 hits
Gene3Di2.60.40.10, 6 hits
InterProiView protein in InterPro
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR011009 Kinase-like_dom_sf
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
PfamiView protein in Pfam
PF00041 fn3, 3 hits
PF10430 Ig_Tie2_1, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00181 EGF, 3 hits
SM00060 FN3, 3 hits
SM00220 S_TKc, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
SSF49265 SSF49265, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTIE2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q02763
Secondary accession number(s): A8K6W0
, B4DH20, B4DHD3, D3DRK5, E7EWI2, Q5TCU2, Q8IV34
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: December 16, 2008
Last modified: May 8, 2019
This is version 210 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program