Kinase insert domain receptor

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KDR
PDB 1vr2 EBI.jpg
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesKDR, CD309, FLK1, VEGFR, VEGFR2, Kinase insert domain receptor
External IDsMGI: 96683 HomoloGene: 55639 GeneCards: KDR
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for KDR
Genomic location for KDR
Band4q12Start55,078,259 bp[1]
End55,125,595 bp[1]
RNA expression pattern
PBB GE KDR 203934 at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002253

NM_010612
NM_001363216

RefSeq (protein)

NP_002244

NP_034742
NP_001350145

Location (UCSC)Chr 4: 55.08 – 55.13 MbChr 5: 75.93 – 75.98 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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[edit]

Kinase insert domain receptor has been shown to interact with SHC2,[5] Annexin A5[6] and SHC1.[7][8]

See also[edit]

Further reading[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000128052 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000062960 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ 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 1220983Freely accessible. PMID 10749680. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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.