FLT1
entrez
2321
canonical
uniprot
P17948
canonical
ensembl
ENSG00000102755
resolver
ensp
ENSP00000282397
resolver
ensp
ENSP00000437631
resolver
ensp
ENSP00000442630
resolver
ensp
ENSP00000484039
resolver
genesymbol
FLT1
resolver
genesymbol_syn
FLT
resolver
genesymbol_syn
FRT
resolver
genesymbol_syn
VEGFR1
resolver
hgnc
HGNC:3763
resolver
uniprot
A3E342
resolver
uniprot
A3E344
resolver
uniprot
A8KA71
resolver
uniprot
B0LPF1
resolver
uniprot
B2BF46
resolver
uniprot
B2BF47
resolver
uniprot
B2BF48
resolver
uniprot
B3FR89
resolver
uniprot
B5A923
resolver
uniprot
F5H5L6
resolver
uniprot
O60722
resolver
uniprot
P16057
resolver
uniprot
Q12954
resolver
uniprot_entry
VGFR1_HUMAN
resolver
uniprot_sec
A3E342
resolver
uniprot_sec
A3E344
resolver
uniprot_sec
A8KA71
resolver
uniprot_sec
B0LPF1
resolver
uniprot_sec
B2BF46
resolver
uniprot_sec
B2BF47
resolver
uniprot_sec
B2BF48
resolver
uniprot_sec
B3FR89
resolver
uniprot_sec
B5A923
resolver
uniprot_sec
F5H5L6
resolver
uniprot_sec
O60722
resolver
uniprot_sec
P16057
resolver
uniprot_sec
Q12954
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFB or PGF leads to dimerization and activation by autophosphorylation on tyrosine residues.
uniprot
proteins
amino_acid_sequence
MVSYWDTGVLLCALLSCLLLTGSSSGSKLKDPELSLKGTQHIMQAGQTLHLQCRGEAAHKWSLPEMVSKESERLSITKSACGRNGKQFCSTLTLNTAQANHTGFYSCKYLAVPTSKKKETESAIYIFISDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTIIDVQISTPRPVKLLRGHTLVLNCTATTPLNTRVQMTWSYPDEKNKRASVRRRIDQSNSHANIFYSVLTIDKMQNKDKGLYTCRVRSGPSFKSVNTSVHIYDKAFITVKHRKQQVLETVAGKRSYRLSMKVKAFPSPEVVWLKDGLPATEKSARYLTRGYSLIIKDVTEEDAGNYTILLSIKQSNVFKNLTATLIVNVKPQIYEKAVSSFPDPALYPLGSRQILTCTAYGIPQPTIKWFWHPCNHNHSEARCDFCSNNEESFILDADSNMGNRIESITQRMAIIEGKNKMASTLVVADSRISGIYICIASNKVGTVGRNISFYITDVPNGFHVNLEKMPTEGEDLKLSCTVNKFLYRDVTWILLRTVNNRTMHYSISKQKMAITKEHSITLNLTIMNVSLQDSGTYACRARNVYTGEEILQKKEITIRDQEAPYLLRNLSDHTVAISSSTTLDCHANGVPEPQITWFKNNHKIQQEPGIILGPGSSTLFIERVTEEDEGVYHCKATNQKGSVESSAYLTVQGTSDKSNLELITLTCTCVAATLFWLLLTLFIRKMKRSSSEIKTDYLSIIMDPDEVPLDEQCERLPYDASKWEFARERLKLGKSLGRGAFGKVVQASAFGIKKSPTCRTVAVKMLKEGATASEYKALMTELKILTHIGHHLNVVNLLGACTKQGGPLMVIVEYCKYGNLSNYLKSKRDLFFLNKDAALHMEPKKEKMEPGLEQGKKPRLDSVTSSESFASSGFQEDKSLSDVEEEEDSDGFYKEPITMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDTRLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGGSPYPGVQMDEDFCSRLREGMRMRAPEYSTPEIYQIMLDCWHRDPKERPRFAELVEKLGDLLQANVQQDGKDYIPINAILTGNSGFTYSTPAFSEDFFKESISAPKFNSGSSDDVRYVNAFKFMSLERIKTFEELLPNATSMFDDYQGDSSTLLASPMLKRFTWTDSKPKASLKIDLRVTSKSKESGLSDVSRPSFCHSSCGHVSEGKRRFTYDHAELERKIACCSPPPDYNSVVLYSTPPI
uniprot
proteins
disease_involvement
DISEASE: Note=Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages.; DISEASE: Note=Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Acts as a positive regulator of postnatal retinal hyaloid vessel regression (By similarity). May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1 (PubMed:16685275). {ECO:0000250|UniProtKB:P35969, ECO:0000269|PubMed:11141500, ECO:0000269|PubMed:11312102, ECO:0000269|PubMed:11811792, ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:14633857, ECO:0000269|PubMed:15735759, ECO:0000269|PubMed:16685275, ECO:0000269|PubMed:18079407, ECO:0000269|PubMed:18515749, ECO:0000269|PubMed:18583712, ECO:0000269|PubMed:18593464, ECO:0000269|PubMed:20512933, ECO:0000269|PubMed:20551949, ECO:0000269|PubMed:21752276, ECO:0000269|PubMed:7824266, ECO:0000269|PubMed:8248162, ECO:0000269|PubMed:8605350, ECO:0000269|PubMed:9299537, ECO:0000269|Ref.11}.; FUNCTION: [Isoform 1]: Phosphorylates PLCG. {ECO:0000269|PubMed:9299537}.; FUNCTION: [Isoform 2]: May function as decoy receptor for VEGFA. {ECO:0000269|PubMed:21752276}.; FUNCTION: [Isoform 3]: May function as decoy receptor for VEGFA. {ECO:0000269|PubMed:21752276}.; FUNCTION: [Isoform 4]: May function as decoy receptor for VEGFA. {ECO:0000269|PubMed:21752276}.; FUNCTION: [Isoform 7]: Has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion. {ECO:0000269|PubMed:20512933}.
uniprot
proteins
mass_dalton
150769
uniprot
proteins
mutagenesis
MUTAGEN 767; /note="V->A: Abolishes proteolytic cleavage by PSEN1."; /evidence="ECO:0000269|PubMed:22016384"; MUTAGEN 861; /note="K->M: Abolishes enzyme activity. Abolishes interaction with PLCG."; /evidence="ECO:0000269|PubMed:9299537"; MUTAGEN 914; /note="Y->F: Reduces phosphorylation at other tyrosine residues."; /evidence="ECO:0000269|PubMed:9722576"; MUTAGEN 1050; /note="N->D: Strongly increases kinase activity. Increases activity in promoting proliferation of endothelial cells."; /evidence="ECO:0000269|PubMed:16286478"; MUTAGEN 1169; /note="Y->F: Loss of phosphorylation site. Abolishes interaction with PLCG."; /evidence="ECO:0000269|PubMed:9299537"; MUTAGEN 1213; /note="Y->F: Loss of phosphorylation site. Abolishes interaction with PIK3R1."; /evidence="ECO:0000269|PubMed:9722576"; MUTAGEN 1242; /note="Y->F: Loss of phosphorylation site."; /evidence="ECO:0000269|PubMed:9722576"; MUTAGEN 1327; /note="Y->F: Loss of phosphorylation site."; /evidence="ECO:0000269|PubMed:9722576"; MUTAGEN 1333; /note="Y->F: Loss of phosphorylation site. Abolishes interaction with CBL."; /evidence="ECO:0000269|PubMed:15001553, ECO:0000269|PubMed:9722576
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:10471394, ECO:0000269|PubMed:11513746}.; PTM: Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation. {ECO:0000269|PubMed:15001553}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-1169 is important for interaction with PLCG. Phosphorylation at Tyr-1213 is important for interaction with PIK3R1, PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1333 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB. {ECO:0000269|PubMed:11513746, ECO:0000269|PubMed:12796773, ECO:0000269|PubMed:9299537, ECO:0000269|PubMed:9600074, ECO:0000269|PubMed:9722576}.
uniprot
proteins
protein_family
CSF-1/PDGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10471394
uniprot
proteins
pubmed
10543948
uniprot
proteins
pubmed
11141500
uniprot
proteins
pubmed
11312102
uniprot
proteins
pubmed
11513746
uniprot
proteins
pubmed
11811792
uniprot
proteins
pubmed
12796773
uniprot
proteins
pubmed
14633857
uniprot
proteins
pubmed
14684734
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15001553
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15735759
uniprot
proteins
pubmed
16286478
uniprot
proteins
pubmed
16685275
uniprot
proteins
pubmed
17002866
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18079407
uniprot
proteins
pubmed
18515749
uniprot
proteins
pubmed
18583712
uniprot
proteins
pubmed
18593464
uniprot
proteins
pubmed
18680722
uniprot
proteins
pubmed
19230644
uniprot
proteins
pubmed
19761875
uniprot
proteins
pubmed
20127948
uniprot
proteins
pubmed
20501651
uniprot
proteins
pubmed
20512933
uniprot
proteins
pubmed
20551949
uniprot
proteins
pubmed
21212275
uniprot
proteins
pubmed
21558755
uniprot
proteins
pubmed
2158038
uniprot
proteins
pubmed
21711246
uniprot
proteins
pubmed
21752276
uniprot
proteins
pubmed
22016384
uniprot
proteins
pubmed
3040650
uniprot
proteins
pubmed
7824266
uniprot
proteins
pubmed
8248162
uniprot
proteins
pubmed
8605350
uniprot
proteins
pubmed
9299537
uniprot
proteins
pubmed
9393862
uniprot
proteins
pubmed
9600074
uniprot
proteins
pubmed
9722576
uniprot
proteins
sequence_length
1338
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Endosome. Note=Autophosphorylation promotes ubiquitination and endocytosis.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:8248162}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 759..780; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins