TEK tyrosine kinase

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TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal)
File:PBB Protein TEK image.jpg
PDB rendering based on 1fvr.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols TEK ; CD202B; TIE-2; TIE2; VMCM; VMCM1
External IDs Template:OMIM5 Template:MGI HomoloGene397
RNA expression pattern
File:PBB GE TEK 206702 at tn.png
File:PBB GE TEK 217711 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal), also known as TEK, is a human gene.

TEK has also recently been designated CD202B (cluster of differentiation 202B).

The TEK receptor tyrosine kinase is expressed almost exclusively in endothelial cells in mice, rats, and humans. This receptor possesses a unique extracellular domain containing 2 immunoglobulin-like loops separated by 3 epidermal growth factor-like repeats that are connected to 3 fibronectin type III-like repeats. The ligand for the receptor is angiopoietin-1. Defects in TEK are associated with inherited venous malformations; the TEK signaling pathway appears to be critical for endothelial cell-smooth muscle cell communication in venous morphogenesis. TEK is closely related to the TIE receptor tyrosine kinase.[1]

References

  1. "Entrez Gene: TEK TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal)".

Further reading

  • Partanen J, Armstrong E, Mäkelä TP; et al. (1992). "A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains". Mol. Cell. Biol. 12 (4): 1698–707. PMID 1312667.
  • Huang L, Turck CW, Rao P, Peters KG (1995). "GRB2 and SH-PTP2: potentially important endothelial signaling molecules downstream of the TEK/TIE2 receptor tyrosine kinase". Oncogene. 11 (10): 2097–103. PMID 7478529.
  • Deans JP, Kalt L, Ledbetter JA; et al. (1995). "Association of 75/80-kDa phosphoproteins and the tyrosine kinases Lyn, Fyn, and Lck with the B cell molecule CD20. Evidence against involvement of the cytoplasmic regions of CD20". J. Biol. Chem. 270 (38): 22632–8. PMID 7545683.
  • Gallione CJ, Pasyk KA, Boon LM; et al. (1995). "A gene for familial venous malformations maps to chromosome 9p in a second large kindred". J. Med. Genet. 32 (3): 197–9. PMID 7783168.
  • Robertson NG, Khetarpal U, Gutiérrez-Espeleta GA; et al. (1995). "Isolation of novel and known genes from a human fetal cochlear cDNA library using subtractive hybridization and differential screening". Genomics. 23 (1): 42–50. doi:10.1006/geno.1994.1457. PMID 7829101.
  • Boon LM, Mulliken JB, Vikkula M; et al. (1995). "Assignment of a locus for dominantly inherited venous malformations to chromosome 9p". Hum. Mol. Genet. 3 (9): 1583–7. PMID 7833915.
  • Dumont DJ, Anderson L, Breitman ML, Duncan AM (1995). "Assignment of the endothelial-specific protein receptor tyrosine kinase gene (TEK) to human chromosome 9p21". Genomics. 23 (2): 512–3. doi:10.1006/geno.1994.1536. PMID 7835909.
  • Ziegler SF, Bird TA, Schneringer JA; et al. (1993). "Molecular cloning and characterization of a novel receptor protein tyrosine kinase from human placenta". Oncogene. 8 (3): 663–70. PMID 8382358.
  • Davis S, Aldrich TH, Jones PF; et al. (1997). "Isolation of angiopoietin-1, a ligand for the TIE2 receptor, by secretion-trap expression cloning". Cell. 87 (7): 1161–9. PMID 8980223.
  • Suri C, Jones PF, Patan S; et al. (1997). "Requisite role of angiopoietin-1, a ligand for the TIE2 receptor, during embryonic angiogenesis". Cell. 87 (7): 1171–80. PMID 8980224.
  • Vikkula M, Boon LM, Carraway KL; et al. (1997). "Vascular dysmorphogenesis caused by an activating mutation in the receptor tyrosine kinase TIE2". Cell. 87 (7): 1181–90. PMID 8980225.
  • Witzenbichler B, Maisonpierre PC, Jones P; et al. (1998). "Chemotactic properties of angiopoietin-1 and -2, ligands for the endothelial-specific receptor tyrosine kinase Tie2". J. Biol. Chem. 273 (29): 18514–21. PMID 9660821.
  • Asahara T, Chen D, Takahashi T; et al. (1998). "Tie2 receptor ligands, angiopoietin-1 and angiopoietin-2, modulate VEGF-induced postnatal neovascularization". Circ. Res. 83 (3): 233–40. PMID 9710115.
  • Sato A, Iwama A, Takakura N; et al. (1998). "Characterization of TEK receptor tyrosine kinase and its ligands, Angiopoietins, in human hematopoietic progenitor cells". Int. Immunol. 10 (8): 1217–27. PMID 9723709.
  • Jones N, Dumont DJ (1998). "The Tek/Tie2 receptor signals through a novel Dok-related docking protein, Dok-R". Oncogene. 17 (9): 1097–108. doi:10.1038/sj.onc.1202115. PMID 9764820.
  • De Sepulveda P, Okkenhaug K, Rose JL; et al. (1999). "Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation". EMBO J. 18 (4): 904–15. doi:10.1093/emboj/18.4.904. PMID 10022833.
  • Valenzuela DM, Griffiths JA, Rojas J; et al. (1999). "Angiopoietins 3 and 4: diverging gene counterparts in mice and humans". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 1904–9. PMID 10051567.
  • Calvert JT, Riney TJ, Kontos CD; et al. (1999). "Allelic and locus heterogeneity in inherited venous malformations". Hum. Mol. Genet. 8 (7): 1279–89. PMID 10369874.
  • Jones N, Master Z, Jones J; et al. (1999). "Identification of Tek/Tie2 binding partners. Binding to a multifunctional docking site mediates cell survival and migration". J. Biol. Chem. 274 (43): 30896–905. PMID 10521483.
  • Fachinger G, Deutsch U, Risau W (1999). "Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2". Oncogene. 18 (43): 5948–53. doi:10.1038/sj.onc.1202992. PMID 10557082.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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