Kinase insert domain receptor

Kinase insert domain receptor (a type III receptor tyrosine kinase)
Available structures
	1y6a, 1y6b
Identifiers
Symbols	KDR; CD309; FLK1; VEGFR; VEGFR2
External IDs	OMIM: 191306 MGI: 96683 HomoloGene: 55639
Gene ontology
Molecular function	• nucleotide binding; • receptor activity; • vascular endothelial growth factor receptor activity; • protein binding; • ATP binding; • transferase activity;
Cellular component	• integral to plasma membrane; • membrane;
Biological process	• angiogenesis; • vasculogenesis; • protein amino acid phosphorylation; • transmembrane receptor protein tyrosine kinase signaling pathway; • multicellular organismal development; • cell migration; • hemopoiesis; • cell fate commitment; • endothelial cell differentiation;
RNA expression pattern
	More reference expression data
Orthologs
NP_002244 (protein)	XP_990085 (protein)

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Kinase insert domain receptor (a type III receptor tyrosine kinase) is a VEGF receptor. KDR is the human gene encoding it. KDR has also been designated as CD309 (cluster of differentiation 309). Flk1 is the abbreviation for fetal liver kinase 1.

[edit] Interactions

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

[edit] See also

[edit] Further reading

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: 201–5; discussion 205–7. 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. PMID 16835467.

[edit] References

^ Warner, A J; Lopez-Dee J, Knight E L, Feramisco J R, Prigent S A (Apr. 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. ISSN 0264-6021. PMID 10749680.
^ 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.
^ Zanetti, Adriana; Lampugnani Maria Grazia, Balconi Giovanna, Breviario Ferruccio, Corada Monica, Lanfrancone Luisa, Dejana Elisabetta (Apr. 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. PMID 11950700.
^ 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. ISSN 0888-8809. PMID 10319320.

[edit] External links

MeSH Kinase+insert+domain+receptor

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

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[pmid10749680-0] Warner, A J; Lopez-Dee J, Knight E L, Feramisco J R, Prigent S A (Apr. 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. ISSN 0264-6021. PMID 10749680.

[pmid10329451-1] 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.

[pmid11950700-2] Zanetti, Adriana; Lampugnani Maria Grazia, Balconi Giovanna, Breviario Ferruccio, Corada Monica, Lanfrancone Luisa, Dejana Elisabetta (Apr. 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. PMID 11950700.

[pmid10319320-3] 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. ISSN 0888-8809. PMID 10319320.

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Kinase insert domain receptor

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[edit] Interactions

[edit] See also

[edit] Further reading

[edit] References

[edit] External links

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