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Reviewed, UniProtKB/Swiss-Prot Q02763 (TIE2_HUMAN)

Last modified November 25, 2008. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Angiopoietin-1 receptor
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor TIE-2
      Short name=hTIE2
    Tyrosine-protein kinase receptor TEK
    Tunica interna endothelial cell kinase
    p140 TEK
    CD_antigen=CD202b
Gene names
Name: TEK
Synonyms: TIE2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This protein is a protein tyrosine-kinase transmembrane receptor for angiopoietin 1. It may constitute the earliest mammalian endothelial cell lineage marker. Probably regulates endothelial cell proliferation, differentiation and guides the proper patterning of endothelial cells during blood vessel formation.

Catalytic activity

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

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

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.

Involvement in disease

Defects in TEK are a cause of dominantly inherited venous malformations (VMCM) [MIM:600195]; an error of vascular morphogenesis characterized by dilated, serpiginous channels.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 11241102Angiopoietin-1 receptor
PRO_0000024474

Regions

Topological domain23 – 745723Extracellular Potential
Transmembrane746 – 77025 Potential
Topological domain771 – 1124354Cytoplasmic 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
Domain445 – 53793Fibronectin type-III 1
Domain544 – 63390Fibronectin type-III 2
Domain639 – 73092Fibronectin type-III 3
Domain824 – 1096273Protein kinase
Nucleotide binding830 – 8389ATP By similarity

Sites

Active site9641Proton acceptor By similarity
Binding site8551ATP By similarity

Amino acid modifications

Modified residue9921Phosphotyrosine; by autocatalysis
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Glycosylation3991N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential
Glycosylation5601N-linked (GlcNAc...) Potential
Glycosylation5961N-linked (GlcNAc...) Potential
Glycosylation6491N-linked (GlcNAc...) Potential
Glycosylation6911N-linked (GlcNAc...) Potential
Disulfide bond220 ↔ 233 By similarity
Disulfide bond227 ↔ 240 By similarity
Disulfide bond242 ↔ 251 By similarity

Natural variations

Natural variant1171K → N in breast cancer samples; infiltrating ductal carcinoma; somatic mutation.
VAR_035714
Natural variant1481I → T
VAR_041855
Natural variant2261A → V
VAR_041856
Natural variant4861V → I: dbSNP rs1334811.
VAR_024578
Natural variant6001V → L
VAR_041857
Natural variant6341L → F
VAR_041858
Natural variant6761V → I
VAR_041859
Natural variant7241A → T
VAR_041860
Natural variant8491R → W in VMCM; activating effect.
VAR_006352
Natural variant8831P → A in an ovarian serous carcinoma sample; somatic mutation.
VAR_041861
Natural variant8971Y → S in VMCM; activating effect.
VAR_008716
Natural variant11241A → V in a renal clear cell carcinoma sample; somatic mutation.
VAR_041862

Secondary structure

........................................................................................................................................ 1124
Helix Strand Turn

Details...