Kinase insert domain receptor

KDR
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1VR2, 1Y6A, 1Y6B, 1YWN, 2M59, 2MET, 2MEU, 2OH4, 2P2H, 2P2I, 2QU5, 2QU6, 2RL5, 2X1W, 2X1X, 2XIR, 3B8Q, 3B8R, 3BE2, 3C7Q, 3CJF, 3CJG, 3CP9, 3CPB, 3CPC, 3DTW, 3EFL, 3EWH, 3KVQ, 3S35, 3S36, 3S37, 3U6J, 3VHE, 3VHK, 3VID, 3VNT, 3VO3, 3WZD, 3WZE, 4AG8, 4AGC, 4AGD, 4ASD, 4ASE, 5EW3
Identifiers
Aliases	KDR, CD309, FLK1, VEGFR, VEGFR2, Kinase insert domain receptor
External IDs	MGI: 96683 HomoloGene: 55639 GeneCards: KDR
Targeted by Drug
axitinib, cabozantinib, cediranib, lenvatinib, linifanib, motesanib, nintedanib, pazopanib, regorafenib, semaxanib, sorafenib, sunitinib, tivozanib, vandetanib, vatalanib[1]
Gene ontology Molecular function • transferase activity • Hsp90 protein binding • nucleotide binding • protein kinase activity • signal transducer, downstream of receptor, with protein tyrosine kinase activity • growth factor binding • vascular endothelial growth factor binding • kinase activity • integrin binding • protein binding • ATP binding • transmembrane receptor protein tyrosine kinase activity • vascular endothelial growth factor-activated receptor activity • protein tyrosine kinase activity Cellular component • cytoplasm • integral component of membrane • Golgi apparatus • membrane • integral component of plasma membrane • cytoplasmic, membrane-bounded vesicle • extracellular region • cell junction • early endosome • membrane raft • sorting endosome • cytoplasmic vesicle • nucleus • endosome • plasma membrane • endoplasmic reticulum Biological process • negative regulation of endothelial cell apoptotic process • cell differentiation • positive regulation of protein phosphorylation • positive regulation of mitochondrial fission • positive regulation of endothelial cell proliferation • phosphorylation • extracellular matrix organization • negative regulation of apoptotic process • positive regulation of nitric-oxide synthase biosynthetic process • cell migration involved in sprouting angiogenesis • positive regulation of angiogenesis • vasculogenesis • positive regulation of endothelial cell migration • multicellular organism development • protein phosphorylation • positive regulation of macroautophagy • positive regulation of mitochondrial depolarization • positive regulation of vasculogenesis • embryonic hemopoiesis • endothelium development • regulation of cell shape • positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway • positive regulation of ERK1 and ERK2 cascade • peptidyl-tyrosine autophosphorylation • protein autophosphorylation • positive regulation of focal adhesion assembly • positive regulation of phosphatidylinositol 3-kinase signaling • peptidyl-tyrosine phosphorylation • cellular response to vascular endothelial growth factor stimulus • viral process • calcium-mediated signaling using intracellular calcium source • positive regulation of MAPK cascade • positive regulation of positive chemotaxis • transmembrane receptor protein tyrosine kinase signaling pathway • signal transduction by protein phosphorylation • vascular endothelial growth factor receptor signaling pathway • positive regulation of cell proliferation • angiogenesis • positive regulation of cell migration Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3791	16542
Ensembl	ENSG00000128052	ENSMUSG00000062960
UniProt	P35968	P35918
RefSeq (mRNA)	NM_002253	NM_010612
RefSeq (protein)	NP_002244.1	n/a
Location (UCSC)	Chr 4: 55.08 – 55.13 Mb	Chr 5: 75.93 – 75.98 Mb
PubMed search	[2]	[3]
Wikidata

View/Edit Human

View/Edit Mouse

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).

Interactions

Kinase insert domain receptor has been shown to interact with SHC2,^[4] Annexin A5^[5] and SHC1.^[6][7]

See also

• Cluster of differentiation
• VEGF receptors

Further reading

• 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.
• Wang J, Fu X, Jiang C, Yu L, Wang M, Han W, Liu L, Wang J (2014). "Bone marrow mononuclear cell transplantation promotes therapeutic angiogenesis via upregulation of the VEGF-VEGFR2 signaling pathway in a rat model of vascular dementia.". Behav. Brain Res. 265: 171–180. doi:10.1016/j.bbr.2014.02.033. PMC 4000455. PMID 24589546.
• 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.

References

1. "Drugs that physically interact with Vascular endothelial growth factor receptor 2 view/edit references on wikidata".
2. "Human PubMed Reference:".
3. "Mouse PubMed Reference:".
4. 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.
5. 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.
6. 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.
7. 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

• Kinase insert domain receptor at the US National Library of Medicine Medical Subject Headings (MeSH)

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