To install click the Add extension button. That's it.

The source code for the WIKI 2 extension is being checked by specialists of the Mozilla Foundation, Google, and Apple. You could also do it yourself at any point in time.

4,5
Kelly Slayton
Congratulations on this excellent venture… what a great idea!
Alexander Grigorievskiy
I use WIKI 2 every day and almost forgot how the original Wikipedia looks like.
Live Statistics
English Articles
Improved in 24 Hours
Added in 24 Hours
What we do. Every page goes through several hundred of perfecting techniques; in live mode. Quite the same Wikipedia. Just better.
.
Leo
Newton
Brights
Milds

Kinase insert domain receptor

From Wikipedia, the free encyclopedia

KDR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesKDR, CD309, FLK1, VEGFR, VEGFR2, Kinase insert domain receptor
External IDsOMIM: 191306; MGI: 96683; HomoloGene: 55639; GeneCards: KDR; OMA:KDR - orthologs
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: 76.09 – 76.14 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Kinase insert domain receptor (KDR, a type IV 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).

The Q472H germline KDR genetic variant affects VEGFR-2 phosphorylation and has been found to associate with microvessel density in NSCLC.[5]

YouTube Encyclopedic

  • 1/5
    Views:
    191 897
    415
    18 033
    6 219
    14 176
  • Receptor Tyrosine Kinase | RTK Signalling
  • Receptor Tyrosine Kinases (RTKs) - part 1: Domains
  • Receptor Tyrosine Kinases Part 1
  • Receptor Tyrosine Kinases Part 2
  • Necroptosis | TNF-Alpha Signalling

Transcription

Interactions

Kinase insert domain receptor has been shown to interact with SHC2,[6] Annexin A5[7] and SHC1.[8][9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000128052Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000062960Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Glubb DM, Cerri E, Giese A, Zhang W, Mirza O, Thompson EE, Chen P, Das S, Jassem J, Rzyman W, Lingen MW, Salgia R, Hirsch FR, Dziadziuszko R, Ballmer-Hofer K, Innocenti F (August 2011). "Novel functional germline variants in the VEGF receptor 2 gene and their effect on gene expression and microvessel density in lung cancer". Clinical Cancer Research. 17 (16): 5257–67. doi:10.1158/1078-0432.CCR-11-0379. PMC 3156871. PMID 21712447.
  6. ^ Warner AJ, Lopez-Dee J, Knight EL, Feramisco JR, Prigent SA (April 2000). "The Shc-related adaptor protein, Sck, forms a complex with the vascular-endothelial-growth-factor receptor KDR in transfected cells". The Biochemical Journal. 347 (Pt 2): 501–9. doi:10.1042/0264-6021:3470501. PMC 1220983. PMID 10749680.
  7. ^ Wen Y, Edelman JL, Kang T, Sachs G (May 1999). "Lipocortin V may function as a signaling protein for vascular endothelial growth factor receptor-2/Flk-1". Biochemical and Biophysical Research Communications. 258 (3): 713–21. doi:10.1006/bbrc.1999.0678. PMID 10329451.
  8. ^ Zanetti A, Lampugnani MG, Balconi G, Breviario F, Corada M, Lanfrancone L, Dejana E (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". Arteriosclerosis, Thrombosis, and Vascular Biology. 22 (4): 617–22. doi:10.1161/01.ATV.0000012268.84961.AD. PMID 11950700.
  9. ^ D'Angelo G, Martini JF, Iiri T, Fantl WJ, Martial J, Weiner RI (May 1999). "16K human prolactin inhibits vascular endothelial growth factor-induced activation of Ras in capillary endothelial cells". Molecular Endocrinology. 13 (5): 692–704. doi:10.1210/mend.13.5.0280. PMID 10319320.

Further reading

External links

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


This page was last edited on 18 May 2022, at 11:50
Basis of this page is in Wikipedia. Text is available under the CC BY-SA 3.0 Unported License. Non-text media are available under their specified licenses. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc. WIKI 2 is an independent company and has no affiliation with Wikimedia Foundation.