Kinase insert domain receptor

From Wikipedia, the free encyclopedia
  (Redirected from VEGFR-2)
Jump to: navigation, search
Kinase insert domain receptor (a type III receptor tyrosine kinase)
PDB 1vr2 EBI.jpg
Rendering of 1VR2
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols KDR ; CD309; FLK1; VEGFR; VEGFR2
External IDs OMIM191306 MGI96683 HomoloGene55639 IUPHAR: 1813 ChEMBL: 279 GeneCards: KDR Gene
EC number
RNA expression pattern
PBB GE KDR 203934 at tn.png
More reference expression data
Species Human Mouse
Entrez 3791 16542
Ensembl ENSG00000128052 ENSMUSG00000062960
UniProt P35968 Q8VCD0
RefSeq (mRNA) NM_002253 NM_010612
RefSeq (protein) NP_002244 NP_034742
Location (UCSC) Chr 4:
55.94 – 55.99 Mb
Chr 5:
75.93 – 75.98 Mb
PubMed search [1] [2]

Kinase insert domain receptor (KDR, a type III receptor tyrosine kinase) also known as vascular endothelial growth factor receptor 2 (VEGFR-2) is a VEGF receptor. KDR is the human gene encoding it. KDR has also been designated as CD309 (cluster of differentiation 309). KDR is also known as Flk1 (Fetal Liver Kinase 1).


Kinase insert domain receptor has been shown to interact with SHC2,[1] Annexin A5[2] and SHC1.[3][4]

See also[edit]

Further reading[edit]

  • Holmes K, Roberts OL, Thomas AM, Cross MJ. (October 2007). "Vascular endothelial growth factor receptor-2: structure, function, intracellular signalling and therapeutic inhibition.". Cell Signal. 19 (10): 2003–2012. doi:10.1016/j.cellsig.2007.05.013. PMID 17658244. 
  • Petrova TV, Makinen T, Alitalo K (1999). "Signaling via vascular endothelial growth factor receptors.". Exp. Cell Res. 253 (1): 117–30. doi:10.1006/excr.1999.4707. PMID 10579917. 
  • Sato Y, Kanno S, Oda N et al. (2000). "Properties of two VEGF receptors, Flt-1 and KDR, in signal transduction.". Ann. N. Y. Acad. Sci. 902 (1): 201–5; discussion 205–7. doi:10.1111/j.1749-6632.2000.tb06314.x. PMID 10865839. 
  • Zachary I, Gliki G (2001). "Signaling transduction mechanisms mediating biological actions of the vascular endothelial growth factor family.". Cardiovasc. Res. 49 (3): 568–81. doi:10.1016/S0008-6363(00)00268-6. PMID 11166270. 
  • Vené R, Benelli R, Noonan DM, Albini A (2001). "HIV-Tat dependent chemotaxis and invasion, key aspects of tat mediated pathogenesis.". Clin. Exp. Metastasis 18 (7): 533–8. doi:10.1023/A:1011991906685. PMID 11688957. 
  • Lenton K (2003). "VEGFR-2 (KDR/Flk-1).". J. Biol. Regul. Homeost. Agents 16 (3): 227–32. PMID 12456025. 
  • Matsumoto T, Mugishima H (2006). "Signal transduction via vascular endothelial growth factor (VEGF) receptors and their roles in atherogenesis.". J. Atheroscler. Thromb. 13 (3): 130–5. doi:10.5551/jat.13.130. PMID 16835467. 


  1. ^ Warner, A J; Lopez-Dee J; Knight E L; Feramisco J R; Prigent S A (April 2000). "The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells". Biochem. J. (England) 347 (Pt 2): 501–9. doi:10.1042/0264-6021:3470501. ISSN 0264-6021. PMC 1220983. PMID 10749680. 
  2. ^ Wen, Y; Edelman J L; Kang T; Sachs G (May 1999). "Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1". Biochem. Biophys. Res. Commun. (UNITED STATES) 258 (3): 713–21. doi:10.1006/bbrc.1999.0678. ISSN 0006-291X. PMID 10329451. 
  3. ^ Zanetti, Adriana; Lampugnani Maria Grazia; Balconi Giovanna; Breviario Ferruccio; Corada Monica; Lanfrancone Luisa; Dejana Elisabetta (April 2002). "Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling". Arterioscler. Thromb. Vasc. Biol. (United States) 22 (4): 617–22. doi:10.1161/01.ATV.0000012268.84961.AD. PMID 11950700. 
  4. ^ D'Angelo, G; Martini J F; Iiri T; Fantl W J; Martial J; Weiner R I (May 1999). "16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells". Mol. Endocrinol. (UNITED STATES) 13 (5): 692–704. doi:10.1210/mend.13.5.0280. ISSN 0888-8809. PMID 10319320. 

External links[edit]

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