Open Access Articles- Top Results for FLT1


SymbolsFLT1 ; FLT; FLT-1; VEGFR-1; VEGFR1
External IDsOMIM165070 MGI95558 HomoloGene134179 IUPHAR: 1812 ChEMBL: 1868 GeneCards: FLT1 Gene
EC number2.7.10.1
RNA expression pattern
File:PBB GE FLT1 222033 s at tn.png
More reference expression data
RefSeq (mRNA)NM_001159920NM_010228
RefSeq (protein)NP_001153392NP_034358
Location (UCSC)Chr 13:
28.87 – 29.07 Mb
Chr 5:
147.56 – 147.73 Mb
PubMed search[1][2]

Vascular endothelial growth factor receptor 1 is a protein that in humans is encoded by the FLT1 gene.[1]


Oncogene FLT belongs to the src gene family and is related to oncogene ROS (MIM 165020). Like other members of this family, it shows tyrosine protein kinase activity that is important for the control of cell proliferation and differentiation. The sequence structure of the FLT gene resembles that of the FMS gene (MIM 164770); hence, Yoshida et al. (1987) proposed the name FLT as an acronym for FMS-like tyrosine kinase.[supplied by OMIM][2]


FLT1 has been shown to interact with PLCG1[3] and Vascular endothelial growth factor B.[4][5]

See also


  1. ^ Shibuya M, Yamaguchi S, Yamane A, Ikeda T, Tojo A, Matsushime H et al. (Apr 1990). "Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family". Oncogene 5 (4): 519–24. PMID 2158038. 
  2. ^ "Entrez Gene: FLT1 fms-related tyrosine kinase 1 (vascular endothelial growth factor/vascular permeability factor receptor)". 
  3. ^ Cunningham SA, Arrate MP, Brock TA, Waxham MN (Nov 1997). "Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites". Biochemical and Biophysical Research Communications 240 (3): 635–9. PMID 9398617. doi:10.1006/bbrc.1997.7719. 
  4. ^ Olofsson B, Korpelainen E, Pepper MS, Mandriota SJ, Aase K, Kumar V et al. (Sep 1998). "Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells". Proceedings of the National Academy of Sciences of the United States of America 95 (20): 11709–14. PMC 21705. PMID 9751730. doi:10.1073/pnas.95.20.11709. 
  5. ^ Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M et al. (Jul 1999). "Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1". The Journal of Biological Chemistry 274 (30): 21217–22. PMID 10409677. doi:10.1074/jbc.274.30.21217. 

Further reading


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