# VEGFR1

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Protein-coding gene in the species Homo sapiens

FLT1 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1FLT, 1QSV, 1QSZ, 1QTY, 1RV6, 2XAC, 3HNG, 4CKV, 4CL7, 5EX3 Identifiers Aliases FLT1, FLT, FLT-1, VEGFR-1, VEGFR1, fms related tyrosine kinase 1, vascular endothelial growth factor receptor 1, fms related receptor tyrosine kinase 1 External IDs OMIM: 165070; MGI: 95558; HomoloGene: 134179; GeneCards: FLT1; OMA:FLT1 - orthologs Gene location (Human) Chr. Chromosome 13 (human)[1] Band 13q12.3 Start 28,300,346 bp[1] End 28,495,145 bp[1] Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 G3|5 87.01 cM Start 147,498,414 bp[2] End 147,662,821 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pericardium placenta endothelial cell right ventricle myocardium of left ventricle dorsal motor nucleus of vagus nerve cardia thyroid gland left lobe of thyroid gland internal globus pallidus Top expressed in right lung right lung lobe internal carotid artery myocardium of ventricle muscle of thigh external carotid artery umbilical cord cardiac muscle tissue of left ventricle islet of Langerhans substantia nigra More reference expression data BioGPS More reference expression data Gene ontology Molecular function vascular endothelial growth factor-activated receptor activity transferase activity nucleotide binding protein kinase activity placental growth factor-activated receptor activity kinase activity protein binding transmembrane receptor protein tyrosine kinase activity protein tyrosine kinase activity ATP binding growth factor binding vascular endothelial growth factor binding Cellular component cytoplasm integral component of membrane endosome focal adhesion membrane receptor complex integral component of plasma membrane extracellular region extracellular space plasma membrane actin cytoskeleton Biological process positive regulation of vascular endothelial growth factor receptor signaling pathway cell differentiation blood vessel morphogenesis vascular endothelial growth factor receptor-1 signaling pathway positive regulation of MAP kinase activity monocyte chemotaxis positive regulation of phospholipase C activity transmembrane receptor protein tyrosine kinase signaling pathway vascular endothelial growth factor signaling pathway phosphorylation positive regulation of angiogenesis positive regulation of phosphatidylinositol 3-kinase activity multicellular organism development chemotaxis protein phosphorylation vascular endothelial growth factor receptor signaling pathway embryonic morphogenesis angiogenesis protein autophosphorylation positive regulation of phosphatidylinositol 3-kinase signaling peptidyl-tyrosine phosphorylation cellular response to vascular endothelial growth factor stimulus cell migration positive regulation of MAPK cascade positive regulation of cell population proliferation positive regulation of cell migration sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade negative regulation of vascular endothelial cell proliferation Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 2321 14254 Ensembl ENSG00000102755 ENSMUSG00000029648 UniProt P17948 P35969 RefSeq (mRNA) NM_001159920 NM_001160030 NM_001160031 NM_002019 NM_010228 NM_001363135 RefSeq (protein) NP_001153392 NP_001153502 NP_001153503 NP_002010 NP_034358 NP_001350064 Location (UCSC) Chr 13: 28.3 – 28.5 Mb Chr 5: 147.5 – 147.66 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Vascular endothelial growth factor receptor 1** is a [protein](/source/Protein) that in humans is encoded by the *FLT1* [gene](/source/Gene).[5]

## Function

*FLT1* is a member of [VEGF receptor](/source/VEGF_receptor) gene family. It encodes a [receptor tyrosine kinase](/source/Receptor_tyrosine_kinase) which is activated by [VEGF-A](/source/VEGF-A), [VEGF-B](/source/VEGF-B), and [placental growth factor](/source/Placental_growth_factor). The sequence structure of the *FLT1* gene resembles that of the *FMS* (now *[CSF1R](/source/CSF1R)*) gene; hence, Yoshida et al. (1987) proposed the name FLT as an acronym for FMS-like tyrosine kinase.[6]

The ablation of VEGFR1 by chemical and genetic means has also recently been found to augment the conversion of [white adipose tissue](/source/White_adipose_tissue) to [brown adipose tissue](/source/Brown_adipose_tissue) as well as increase brown adipose [angiogenesis](/source/Angiogenesis) in mice.[7]

Functional genetic variation in *FLT1* (rs9582036) has been found to affect [non-small cell lung cancer](/source/Non-small-cell_lung_carcinoma) survival.[8]

## Interactions

FLT1 has been shown to [interact](/source/Protein-protein_interaction) with [PLCG1](/source/PLCG1)[9] and [vascular endothelial growth factor B](/source/Vascular_endothelial_growth_factor_B) (VEGF-B).[10][11]

## See also

- [VEGF receptors](/source/VEGF_receptors)

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000102755](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000102755) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000029648](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000029648) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=2321). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=14254). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid2158038_5-0)** Shibuya M, Yamaguchi S, Yamane A, Ikeda T, Tojo A, Matsushime H, Sato M (April 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](/source/PMID_(identifier)) [2158038](https://pubmed.ncbi.nlm.nih.gov/2158038).

1. **[^](#cite_ref-6)** ["FLT1 fms related receptor tyrosine kinase 1 \[ Homo sapiens (human) \]"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=2321). [National Center for Biotechnology Information](/source/National_Center_for_Biotechnology_Information).

1. **[^](#cite_ref-7)** Seki T, Hosaka K, Fischer C, Lim S, Andersson P, Abe M, Iwamoto H, Gao Y, Wang X, Fong GH, Cao Y (February 2018). ["Ablation of endothelial VEGFR1 improves metabolic dysfunction by inducing adipose tissue browning"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5789413). *The Journal of Experimental Medicine*. **215** (2): 611–626. [doi](/source/Doi_(identifier)):[10.1084/jem.20171012](https://doi.org/10.1084%2Fjem.20171012). [PMC](/source/PMC_(identifier)) [5789413](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5789413). [PMID](/source/PMID_(identifier)) [29305395](https://pubmed.ncbi.nlm.nih.gov/29305395).

1. **[^](#cite_ref-8)** Glubb DM, Paré-Brunet L, Jantus-Lewintre E, Jiang C, Crona D, Etheridge AS, Mirza O, Zhang W, Seiser EL, Rzyman W, Jassem J, Auman T, Hirsch FR, Owzar K, Camps C, Dziadziuszko R, Innocenti F (July 2015). ["Functional FLT1 Genetic Variation is a Prognostic Factor for Recurrence in Stage I-III Non-Small-Cell Lung Cancer"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4494119). *Journal of Thoracic Oncology*. **10** (7): 1067–75. [doi](/source/Doi_(identifier)):[10.1097/JTO.0000000000000549](https://doi.org/10.1097%2FJTO.0000000000000549). [PMC](/source/PMC_(identifier)) [4494119](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4494119). [PMID](/source/PMID_(identifier)) [26134224](https://pubmed.ncbi.nlm.nih.gov/26134224).

1. **[^](#cite_ref-pmid9398617_9-0)** Cunningham SA, Arrate MP, Brock TA, Waxham MN (November 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. [Bibcode](/source/Bibcode_(identifier)):[1997BBRC..240..635C](https://ui.adsabs.harvard.edu/abs/1997BBRC..240..635C). [doi](/source/Doi_(identifier)):[10.1006/bbrc.1997.7719](https://doi.org/10.1006%2Fbbrc.1997.7719). [PMID](/source/PMID_(identifier)) [9398617](https://pubmed.ncbi.nlm.nih.gov/9398617).

1. **[^](#cite_ref-pmid9751730_10-0)** Olofsson B, Korpelainen E, Pepper MS, Mandriota SJ, Aase K, Kumar V, Gunji Y, Jeltsch MM, Shibuya M, Alitalo K, Eriksson U (September 1998). ["Vascular endothelial growth factor B (VEGF-B) binds to VEGF receptor-1 and regulates plasminogen activator activity in endothelial cells"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21705). *Proceedings of the National Academy of Sciences of the United States of America*. **95** (20): 11709–14. [Bibcode](/source/Bibcode_(identifier)):[1998PNAS...9511709O](https://ui.adsabs.harvard.edu/abs/1998PNAS...9511709O). [doi](/source/Doi_(identifier)):[10.1073/pnas.95.20.11709](https://doi.org/10.1073%2Fpnas.95.20.11709). [PMC](/source/PMC_(identifier)) [21705](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC21705). [PMID](/source/PMID_(identifier)) [9751730](https://pubmed.ncbi.nlm.nih.gov/9751730).

1. **[^](#cite_ref-pmid10409677_11-0)** Makinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, Eriksson U, Alitalo K (July 1999). ["Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1"](https://doi.org/10.1074%2Fjbc.274.30.21217). *The Journal of Biological Chemistry*. **274** (30): 21217–22. [doi](/source/Doi_(identifier)):[10.1074/jbc.274.30.21217](https://doi.org/10.1074%2Fjbc.274.30.21217). [PMID](/source/PMID_(identifier)) [10409677](https://pubmed.ncbi.nlm.nih.gov/10409677).

## Further reading

- Petrova TV, Makinen T, Alitalo K (November 1999). "Signaling via vascular endothelial growth factor receptors". *Experimental Cell Research*. **253** (1): 117–30. [doi](/source/Doi_(identifier)):[10.1006/excr.1999.4707](https://doi.org/10.1006%2Fexcr.1999.4707). [PMID](/source/PMID_(identifier)) [10579917](https://pubmed.ncbi.nlm.nih.gov/10579917).

- Sato Y, Kanno S, Oda N, Abe M, Ito M, Shitara K, Shibuya M (May 2000). "Properties of two VEGF receptors, Flt-1 and KDR, in signal transduction". *Annals of the New York Academy of Sciences*. **902** (1): 201–5, discussion 205–7. [Bibcode](/source/Bibcode_(identifier)):[2000NYASA.902..201S](https://ui.adsabs.harvard.edu/abs/2000NYASA.902..201S). [doi](/source/Doi_(identifier)):[10.1111/j.1749-6632.2000.tb06314.x](https://doi.org/10.1111%2Fj.1749-6632.2000.tb06314.x). [PMID](/source/PMID_(identifier)) [10865839](https://pubmed.ncbi.nlm.nih.gov/10865839). [S2CID](/source/S2CID_(identifier)) [11488629](https://api.semanticscholar.org/CorpusID:11488629).

- Boyd AW, Lackmann M (December 2001). "Signals from Eph and ephrin proteins: a developmental tool kit". *Science's STKE*. **2001** (112): re20. [doi](/source/Doi_(identifier)):[10.1126/stke.2001.112.re20](https://doi.org/10.1126%2Fstke.2001.112.re20). [PMID](/source/PMID_(identifier)) [11741094](https://pubmed.ncbi.nlm.nih.gov/11741094). [S2CID](/source/S2CID_(identifier)) [2952319](https://api.semanticscholar.org/CorpusID:2952319).

- Luttun A, Tjwa M, Carmeliet P (December 2002). "Placental growth factor (PlGF) and its receptor Flt-1 (VEGFR-1): novel therapeutic targets for angiogenic disorders". *Annals of the New York Academy of Sciences*. **979**: 80–93. [doi](/source/Doi_(identifier)):[10.1111/j.1749-6632.2002.tb04870.x](https://doi.org/10.1111%2Fj.1749-6632.2002.tb04870.x). [PMID](/source/PMID_(identifier)) [12543719](https://pubmed.ncbi.nlm.nih.gov/12543719). [S2CID](/source/S2CID_(identifier)) [73356935](https://api.semanticscholar.org/CorpusID:73356935).

- Maynard SE, Venkatesha S, Thadhani R, Karumanchi SA (May 2005). ["Soluble Fms-like tyrosine kinase 1 and endothelial dysfunction in the pathogenesis of preeclampsia"](https://doi.org/10.1203%2F01.PDR.0000159567.85157.B7). *Pediatric Research*. **57** (5 Pt 2): 1R–7R. [doi](/source/Doi_(identifier)):[10.1203/01.PDR.0000159567.85157.B7](https://doi.org/10.1203%2F01.PDR.0000159567.85157.B7). [PMID](/source/PMID_(identifier)) [15817508](https://pubmed.ncbi.nlm.nih.gov/15817508).

- Shibuya M (2007). "Vascular endothelial growth factor receptor-1 (VEGFR-1/Flt-1): a dual regulator for angiogenesis". *Angiogenesis*. **9** (4): 225–30, discussion 231. [doi](/source/Doi_(identifier)):[10.1007/s10456-006-9055-8](https://doi.org/10.1007%2Fs10456-006-9055-8). [PMID](/source/PMID_(identifier)) [17109193](https://pubmed.ncbi.nlm.nih.gov/17109193). [S2CID](/source/S2CID_(identifier)) [20495537](https://api.semanticscholar.org/CorpusID:20495537).

- Widmer M, Villar J, Benigni A, Conde-Agudelo A, Karumanchi SA, Lindheimer M (January 2007). "Mapping the theories of preeclampsia and the role of angiogenic factors: a systematic review". *Obstetrics and Gynecology*. **109** (1): 168–80. [doi](/source/Doi_(identifier)):[10.1097/01.AOG.0000249609.04831.7c](https://doi.org/10.1097%2F01.AOG.0000249609.04831.7c). [PMID](/source/PMID_(identifier)) [17197602](https://pubmed.ncbi.nlm.nih.gov/17197602). [S2CID](/source/S2CID_(identifier)) [24187545](https://api.semanticscholar.org/CorpusID:24187545).

- López-Novoa JM (March 2007). ["Soluble endoglin is an accurate predictor and a pathogenic molecule in pre-eclampsia"](https://doi.org/10.1093%2Fndt%2Fgfl768). *Nephrology, Dialysis, Transplantation*. **22** (3): 712–4. [doi](/source/Doi_(identifier)):[10.1093/ndt/gfl768](https://doi.org/10.1093%2Fndt%2Fgfl768). [PMID](/source/PMID_(identifier)) [17210583](https://pubmed.ncbi.nlm.nih.gov/17210583).

- Poesen K, Lambrechts D, Van Damme P, Dhondt J, Bender F, Frank N, Bogaert E, Claes B, Heylen L, Verheyen A, Raes K, Tjwa M, Eriksson U, Shibuya M, Nuydens R, Van Den Bosch L, Meert T, D'Hooge R, Sendtner M, Robberecht W, Carmeliet P (October 2008). ["Novel role for vascular endothelial growth factor (VEGF) receptor-1 and its ligand VEGF-B in motor neuron degeneration"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6671326). *The Journal of Neuroscience*. **28** (42): 10451–9. [doi](/source/Doi_(identifier)):[10.1523/JNEUROSCI.1092-08.2008](https://doi.org/10.1523%2FJNEUROSCI.1092-08.2008). [PMC](/source/PMC_(identifier)) [6671326](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6671326). [PMID](/source/PMID_(identifier)) [18923022](https://pubmed.ncbi.nlm.nih.gov/18923022).

- Joukov V, Kaipainen A, Jeltsch M, Pajusola K, Olofsson B, Kumar V, Eriksson U, Alitalo K (November 1997). "Vascular endothelial growth factors VEGF-B and VEGF-C". *Journal of Cellular Physiology*. **173** (2): 211–5. [doi](/source/Doi_(identifier)):[10.1002/(SICI)1097-4652(199711)173:2<211::AID-JCP23>3.0.CO;2-H](https://doi.org/10.1002%2F%28SICI%291097-4652%28199711%29173%3A2%3C211%3A%3AAID-JCP23%3E3.0.CO%3B2-H). [PMID](/source/PMID_(identifier)) [9365524](https://pubmed.ncbi.nlm.nih.gov/9365524). [S2CID](/source/S2CID_(identifier)) [2930599](https://api.semanticscholar.org/CorpusID:2930599).

- Kaplan RN, Riba RD, Zacharoulis S, Bramley AH, Vincent L, Costa C, MacDonald DD, Jin DK, Shido K, Kerns SA, Zhu Z, Hicklin D, Wu Y, Port JL, Altorki N, Port ER, Ruggero D, Shmelkov SV, Jensen KK, Rafii S, Lyden D (December 2005). ["VEGFR1-positive haematopoietic bone marrow progenitors initiate the pre-metastatic niche"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2945882). *Nature*. **438** (7069): 820–7. [Bibcode](/source/Bibcode_(identifier)):[2005Natur.438..820K](https://ui.adsabs.harvard.edu/abs/2005Natur.438..820K). [doi](/source/Doi_(identifier)):[10.1038/nature04186](https://doi.org/10.1038%2Fnature04186). [PMC](/source/PMC_(identifier)) [2945882](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2945882). [PMID](/source/PMID_(identifier)) [16341007](https://pubmed.ncbi.nlm.nih.gov/16341007).

v t e PDB gallery 1flt: VEGF IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR 1qsv: THE VEGF-BINDING DOMAIN OF FLT-1, 20 NMR STRUCTURES 1qsz: THE VEGF-BINDING DOMAIN OF FLT-1 (MINIMIZED MEAN) 1qty: VASCULAR ENDOTHELIAL GROWTH FACTOR IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR 1rv6: Crystal Structure of PlGF in Complex with Domain 2 of VEGFR1

v t e Receptors: growth factor receptors Type I cytokine receptor Nerve growth factors Ciliary neurotrophic factor Erythropoietin Receptor protein serine/threonine kinase TGF pathway TGF-beta 1 2 Activin 1 2 Bone morphogenetic protein 1 2 Receptor tyrosine kinase Fibroblast growth factor 1 2 3 4 Nerve growth factors: high affinity Trk TrkA TrkB TrkC Hepatocyte growth factor Somatomedin Insulin-like growth factor 1 ErbB/Epidermal growth factor VEGF 1 2 3 Tumor necrosis factor receptor Nerve growth factors: Low affinity/p75 Ig superfamily Platelet-derived growth factor A B Stem cell factor Other/ungrouped Somatomedin Insulin-like growth factor 2

v t e Protein kinases: tyrosine kinases (EC 2.7.10) Receptor tyrosine kinases (EC 2.7.10.1) Growth factor receptors EGF receptor family EGFR ERBB2 ERBB3 ERBB4 Insulin receptor family IGF1R INSR INSRR PDGF receptor family CSF1R FLT3 KIT PDGFR PDGFRA PDGFRB FGF receptor family FGFR1 FGFR2 FGFR3 FGFR4 VEGF receptor family VEGFR1 VEGFR2 VEGFR3 HGF receptor family MET RON Trk receptor family NTRK1 NTRK2 NTRK3 EPH receptor family EPHA1 EPHA2 EPHA3 EPHA4 EPHA5 EPHA6 EPHA7 EPHA8 EPHB1 EPHB2 EPHB3 EPHB4 EPHB5 EPHB6 EPHX LTK receptor family LTK ALK TIE receptor family TIE TEK ROR receptor family ROR1 ROR2 DDR receptor family DDR1 DDR2 PTK7 receptor family PTK7 RYK receptor family RYK MuSK receptor family MUSK ROS receptor family ROS1 AATYK receptor family AATYK AATYK2 AXL receptor family AXL MER TYRO3 RET receptor family RET uncategorised STYK1 Non-receptor tyrosine kinases (EC 2.7.10.2) ABL family ABL1 ARG ACK family ACK1 TNK1 CSK family CSK MATK FAK family FAK PYK2 FES family FES FER FRK family FRK BRK SRMS JAK family JAK1 JAK2 JAK3 TYK2 SRC-A family SRC FGR FYN YES1 SRC-B family BLK HCK LCK LYN TEC family TEC BMX BTK ITK TXK SYK family SYK ZAP70

v t e Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics Types EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

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Adapted from the Wikipedia article [VEGFR1](https://en.wikipedia.org/wiki/VEGFR1) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/VEGFR1?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.