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Protein

Vascular endothelial growth factor receptor 1

Gene

FLT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. 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. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion.18 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation5 Publications

Enzyme regulationi

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei861ATPPROSITE-ProRule annotation1
Active sitei1022Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi833 – 841ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • growth factor binding Source: UniProtKB
  • placental growth factor-activated receptor activity Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase activity Source: ProtInc
  • vascular endothelial growth factor-activated receptor activity Source: UniProtKB
  • VEGF-A-activated receptor activity Source: UniProtKB
  • VEGF-B-activated receptor activity Source: UniProtKB

GO - Biological processi

  • angiogenesis Source: UniProtKB-KW
  • blood vessel morphogenesis Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • cell migration Source: UniProtKB
  • cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  • embryonic morphogenesis Source: UniProtKB
  • monocyte chemotaxis Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cell proliferation Source: ProtInc
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of phospholipase C activity Source: UniProtKB
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • protein autophosphorylation Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
  • vascular endothelial growth factor receptor-1 signaling pathway Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Chemotaxis, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS02408-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-194306. Neurophilin interactions with VEGF and VEGFR.
R-HSA-195399. VEGF binds to VEGFR leading to receptor dimerization.
SignaLinkiP17948.
SIGNORiP17948.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor receptor 1 (EC:2.7.10.1)
Short name:
VEGFR-1
Alternative name(s):
Fms-like tyrosine kinase 1
Short name:
FLT-1
Tyrosine-protein kinase FRT
Tyrosine-protein kinase receptor FLT
Short name:
FLT
Vascular permeability factor receptor
Gene namesi
Name:FLT1
Synonyms:FLT, FRT, VEGFR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3763. FLT1.

Subcellular locationi

Isoform 1 :
Isoform 2 :
  • Secreted 1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 758ExtracellularSequence analysisAdd BLAST732
Transmembranei759 – 780HelicalSequence analysisAdd BLAST22
Topological domaini781 – 1338CytoplasmicSequence analysisAdd BLAST558

GO - Cellular componenti

  • endosome Source: UniProtKB-SubCell
  • extracellular space Source: ProtInc
  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

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.

Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi767V → A: Abolishes proteolytic cleavage by PSEN1. 1 Publication1
Mutagenesisi861K → M: Abolishes enzyme activity. Abolishes interaction with PLCG. 1 Publication1
Mutagenesisi914Y → F: Reduces phosphorylation at other tyrosine residues. 1 Publication1
Mutagenesisi1050N → D: Strongly increases kinase activity. Increases activity in promoting proliferation of endothelial cells. 1 Publication1
Mutagenesisi1169Y → F: Loss of phosphorylation site. Abolishes interaction with PLCG. 1 Publication1
Mutagenesisi1213Y → F: Loss of phosphorylation site. Abolishes interaction with PIK3R1. 1 Publication1
Mutagenesisi1242Y → F: Loss of phosphorylation site. 1 Publication1
Mutagenesisi1327Y → F: Loss of phosphorylation site. 1 Publication1
Mutagenesisi1333Y → F: Loss of phosphorylation site. Abolishes interaction with CBL. 2 Publications1

Organism-specific databases

DisGeNETi2321.
OpenTargetsiENSG00000102755.
PharmGKBiPA28180.

Chemistry databases

ChEMBLiCHEMBL1868.
DrugBankiDB06626. Axitinib.
DB09078. Lenvatinib.
DB09079. Nintedanib.
DB06589. Pazopanib.
DB08896. Regorafenib.
DB00398. Sorafenib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGYi1812.

Polymorphism and mutation databases

BioMutaiFLT1.
DMDMi143811474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000001676827 – 1338Vascular endothelial growth factor receptor 1Add BLAST1312

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi53 ↔ 107PROSITE-ProRule annotation
Glycosylationi100N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi158 ↔ 207
Glycosylationi164N-linked (GlcNAc...)Sequence analysis1
Glycosylationi196N-linked (GlcNAc...)Sequence analysis1
Glycosylationi251N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi252 ↔ 311PROSITE-ProRule annotation
Glycosylationi323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi402N-linked (GlcNAc...)Sequence analysis1
Glycosylationi417N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi454 ↔ 535PROSITE-ProRule annotation
Glycosylationi474N-linked (GlcNAc...)Sequence analysis1
Glycosylationi547N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi577 ↔ 636PROSITE-ProRule annotation
Glycosylationi597N-linked (GlcNAc...)Sequence analysis1
Glycosylationi620N-linked (GlcNAc...)Sequence analysis1
Glycosylationi625N-linked (GlcNAc...)Sequence analysis1
Glycosylationi666N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi682 ↔ 731PROSITE-ProRule annotation
Modified residuei914Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1053Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1169Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1213Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei1242Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1309Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1327Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1333Phosphotyrosine; by autocatalysis1 Publication1

Post-translational modificationi

N-glycosylated.2 Publications
Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation.1 Publication
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.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei767 – 768Cleavage; by PSEN1Curated2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP17948.
MaxQBiP17948.
PaxDbiP17948.
PeptideAtlasiP17948.
PRIDEiP17948.

PTM databases

iPTMnetiP17948.
PhosphoSitePlusiP17948.
UniCarbKBiP17948.

Expressioni

Tissue specificityi

Detected in normal lung, but also in placenta, liver, kidney, heart and brain tissues. Specifically expressed in most of the vascular endothelial cells, and also expressed in peripheral blood monocytes. Isoform 2 is strongly expressed in placenta. Isoform 3 is expressed in corneal epithelial cells (at protein level). Isoform 3 is expressed in vascular smooth muscle cells (VSMC).2 Publications

Inductioni

Up-regulated in coculture of VSMC/endothelial cell (EC) or by direct exposure to VEGF of VSMC monoculture. Up-regulated from the second trimester of pregnancy to the term and in the placenta of women with preeclampsia (PE). Up-regulated in monocytes exposed to bacterial lipopolysaccharide (LPS).2 Publications

Gene expression databases

BgeeiENSG00000102755.
CleanExiHS_FLT1.
ExpressionAtlasiP17948. baseline and differential.
GenevisibleiP17948. HS.

Organism-specific databases

HPAiCAB068189.
CAB068190.
HPA011740.
HPA014290.

Interactioni

Subunit structurei

Interacts with VEGFA, VEGFB and PGF. Monomer in the absence of bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA, VEGFB and PGF. Can also form a heterodimer with KDR. Interacts (when tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts also with PTPRB. Interacts with RACK1. Identified in a complex with CBL and CD2AP.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBLP226812EBI-1026718,EBI-518228
CRKLP461099EBI-1026718,EBI-910
CTNNB1P352222EBI-1026718,EBI-491549
HCKP086312EBI-1026718,EBI-346340
HSPG2P981602EBI-6530464,EBI-6896607
PGFP497632EBI-1026718,EBI-1037633
PIK3R1P279862EBI-1026718,EBI-79464
PLCG1P191742EBI-1026718,EBI-79387
PTK2Q053972EBI-1026718,EBI-702142
PTPN11Q061242EBI-1026718,EBI-297779
PTPRJQ129132EBI-1026718,EBI-2264500
VEGFAP156924EBI-1026718,EBI-1026643
VEGFAP15692-43EBI-1026718,EBI-1026691

GO - Molecular functioni

  • growth factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108609. 13 interactors.
DIPiDIP-643N.
IntActiP17948. 30 interactors.
MINTiMINT-127610.
STRINGi9606.ENSP00000282397.

Chemistry databases

BindingDBiP17948.

Structurei

Secondary structure

11338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni130 – 132Combined sources3
Beta strandi135 – 137Combined sources3
Beta strandi140 – 142Combined sources3
Beta strandi144 – 148Combined sources5
Beta strandi150 – 152Combined sources3
Beta strandi154 – 156Combined sources3
Beta strandi160 – 162Combined sources3
Helixi163 – 165Combined sources3
Beta strandi168 – 171Combined sources4
Turni172 – 174Combined sources3
Beta strandi175 – 177Combined sources3
Beta strandi181 – 187Combined sources7
Turni188 – 190Combined sources3
Beta strandi191 – 196Combined sources6
Helixi199 – 201Combined sources3
Beta strandi203 – 211Combined sources9
Beta strandi214 – 224Combined sources11
Helixi806 – 809Combined sources4
Helixi817 – 820Combined sources4
Helixi824 – 826Combined sources3
Beta strandi827 – 835Combined sources9
Beta strandi837 – 848Combined sources12
Helixi849 – 851Combined sources3
Beta strandi854 – 863Combined sources10
Helixi869 – 883Combined sources15
Beta strandi894 – 898Combined sources5
Beta strandi906 – 910Combined sources5
Helixi917 – 922Combined sources6
Helixi996 – 1014Combined sources19
Turni1015 – 1017Combined sources3
Helixi1025 – 1027Combined sources3
Beta strandi1028 – 1030Combined sources3
Helixi1032 – 1034Combined sources3
Beta strandi1036 – 1038Combined sources3
Helixi1042 – 1044Combined sources3
Turni1047 – 1049Combined sources3
Beta strandi1053 – 1055Combined sources3
Helixi1063 – 1065Combined sources3
Helixi1068 – 1073Combined sources6
Helixi1078 – 1093Combined sources16
Helixi1107 – 1113Combined sources7
Turni1114 – 1116Combined sources3
Helixi1127 – 1136Combined sources10
Helixi1141 – 1143Combined sources3
Helixi1147 – 1157Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FLTX-ray1.70X/Y132-226[»]
1QSVNMR-A129-229[»]
1QSZNMR-A129-229[»]
1QTYX-ray2.70T/U/X/Y129-229[»]
1RV6X-ray2.45X/Y130-229[»]
2XACX-ray2.71C/X129-226[»]
3HNGX-ray2.70A801-1158[»]
4CKVX-ray2.06X132-225[»]
4CL7X-ray2.00A/B/C/D132-225[»]
5ABDX-ray2.00E/I/X132-226[»]
5EX3X-ray2.41D827-835[»]
ProteinModelPortaliP17948.
SMRiP17948.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17948.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 123Ig-like C2-type 1Add BLAST92
Domaini151 – 214Ig-like C2-type 2Add BLAST64
Domaini230 – 327Ig-like C2-type 3Add BLAST98
Domaini335 – 421Ig-like C2-type 4Add BLAST87
Domaini428 – 553Ig-like C2-type 5Add BLAST126
Domaini556 – 654Ig-like C2-type 6Add BLAST99
Domaini661 – 747Ig-like C2-type 7Add BLAST87
Domaini827 – 1158Protein kinasePROSITE-ProRule annotationAdd BLAST332

Domaini

The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFA binding.2 Publications

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP17948.
KOiK05096.
OMAiILTHIGH.
OrthoDBiEOG091G01TL.
PhylomeDBiP17948.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009135. VEGFR1_rcpt.
[Graphical view]
PfamiPF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01833. VEGFRECEPTR1.
SMARTiSM00409. IG. 7 hits.
SM00408. IGc2. 5 hits.
SM00406. IGv. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 6 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P17948-1) [UniParc]FASTAAdd to basket
Also known as: Flt1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH
60 70 80 90 100
LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN
110 120 130 140 150
HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE
160 170 180 190 200
GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK
210 220 230 240 250
EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL
260 270 280 290 300
NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK
310 320 330 340 350
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK
360 370 380 390 400
RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA
410 420 430 440 450
GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ
460 470 480 490 500
ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN
510 520 530 540 550
RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF
560 570 580 590 600
YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM
610 620 630 640 650
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK
660 670 680 690 700
KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK
710 720 730 740 750
IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG
760 770 780 790 800
TSDKSNLELI TLTCTCVAAT LFWLLLTLFI RKMKRSSSEI KTDYLSIIMD
810 820 830 840 850
PDEVPLDEQC ERLPYDASKW EFARERLKLG KSLGRGAFGK VVQASAFGIK
860 870 880 890 900
KSPTCRTVAV KMLKEGATAS EYKALMTELK ILTHIGHHLN VVNLLGACTK
910 920 930 940 950
QGGPLMVIVE YCKYGNLSNY LKSKRDLFFL NKDAALHMEP KKEKMEPGLE
960 970 980 990 1000
QGKKPRLDSV TSSESFASSG FQEDKSLSDV EEEEDSDGFY KEPITMEDLI
1010 1020 1030 1040 1050
SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN
1060 1070 1080 1090 1100
PDYVRKGDTR LPLKWMAPES IFDKIYSTKS DVWSYGVLLW EIFSLGGSPY
1110 1120 1130 1140 1150
PGVQMDEDFC SRLREGMRMR APEYSTPEIY QIMLDCWHRD PKERPRFAEL
1160 1170 1180 1190 1200
VEKLGDLLQA NVQQDGKDYI PINAILTGNS GFTYSTPAFS EDFFKESISA
1210 1220 1230 1240 1250
PKFNSGSSDD VRYVNAFKFM SLERIKTFEE LLPNATSMFD DYQGDSSTLL
1260 1270 1280 1290 1300
ASPMLKRFTW TDSKPKASLK IDLRVTSKSK ESGLSDVSRP SFCHSSCGHV
1310 1320 1330
SEGKRRFTYD HAELERKIAC CSPPPDYNSV VLYSTPPI
Length:1,338
Mass (Da):150,769
Last modified:April 3, 2007 - v2
Checksum:iFF3381EEFAF0787C
GO
Isoform 2 (identifier: P17948-2) [UniParc]FASTAAdd to basket
Also known as: sFlt1

The sequence of this isoform differs from the canonical sequence as follows:
     657-687: DQEAPYLLRNLSDHTVAISSSTTLDCHANGV → GEHCNKKAVFSRISKFKSTRNDCTTQSNVKH
     688-1338: Missing.

Show »
Length:687
Mass (Da):77,474
Checksum:i3F73F4942469DA36
GO
Isoform 3 (identifier: P17948-3) [UniParc]FASTAAdd to basket
Also known as: sFlt1-14

The sequence of this isoform differs from the canonical sequence as follows:
     706-733: GIILGPGSSTLFIERVTEEDEGVYHCKA → ELYTSTSPSSSSSSPLSSSSSSSSSSSS
     734-1338: Missing.

Show »
Length:733
Mass (Da):82,124
Checksum:i67B7F8BC1D30CD9E
GO
Isoform 4 (identifier: P17948-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     518-541: MASTLVVADSRISGIYICIASNKV → LPPANSSFMLPPTSFSSNYFHFLP
     542-1338: Missing.

Show »
Length:541
Mass (Da):60,917
Checksum:i50BCDAACB69B0EA2
GO
Isoform 5 (identifier: P17948-5) [UniParc]FASTAAdd to basket
Also known as: i15

The sequence of this isoform differs from the canonical sequence as follows:
     1-782: Missing.

Show »
Length:556
Mass (Da):62,954
Checksum:i9150507FBDF43B24
GO
Isoform 6 (identifier: P17948-6) [UniParc]FASTAAdd to basket
Also known as: i18

The sequence of this isoform differs from the canonical sequence as follows:
     1-875: Missing.

Show »
Length:463
Mass (Da):52,613
Checksum:i7D3D572623A1124E
GO
Isoform 7 (identifier: P17948-7) [UniParc]FASTAAdd to basket
Also known as: i21

The sequence of this isoform differs from the canonical sequence as follows:
     1-995: Missing.

Show »
Length:343
Mass (Da):39,148
Checksum:iB7800AF7311BF0D6
GO
Isoform 8 (identifier: P17948-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MVSYWDT → MNSDLLV
     8-984: Missing.

Show »
Length:361
Mass (Da):41,175
Checksum:i34E2B38DE128BA53
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti490F → S in AAC16449 (PubMed:10471394).Curated1
Sequence conflicti779F → L in CAA35946 (PubMed:2158038).Curated1
Sequence conflicti1029L → F in ABI53803 (PubMed:20512933).Curated1
Sequence conflicti1029L → F in ABI53804 (PubMed:20512933).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04204560K → T.1 PublicationCorresponds to variant rs56409818dbSNPEnsembl.1
Natural variantiVAR_049719128I → L.Corresponds to variant rs35073261dbSNPEnsembl.1
Natural variantiVAR_042046144E → K.1 PublicationCorresponds to variant rs55974987dbSNPEnsembl.1
Natural variantiVAR_042047281R → Q.1 PublicationCorresponds to variant rs55687105dbSNPEnsembl.1
Natural variantiVAR_042048422L → I in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042049781R → Q in a glioma low grade oligodendroglioma sample; somatic mutation. 1 PublicationCorresponds to variant rs553261958dbSNPEnsembl.1
Natural variantiVAR_042050938M → V.1 PublicationCorresponds to variant rs35549791dbSNPEnsembl.1
Natural variantiVAR_042051982E → A.1 PublicationCorresponds to variant rs35832528dbSNPEnsembl.1
Natural variantiVAR_0420521061L → V in a bladder transitional cell carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0419831 – 995Missing in isoform 7. 1 PublicationAdd BLAST995
Alternative sequenceiVSP_0419841 – 875Missing in isoform 6. 1 PublicationAdd BLAST875
Alternative sequenceiVSP_0419851 – 782Missing in isoform 5. 1 PublicationAdd BLAST782
Alternative sequenceiVSP_0477591 – 7MVSYWDT → MNSDLLV in isoform 8. 1 Publication7
Alternative sequenceiVSP_0477608 – 984Missing in isoform 8. 1 PublicationAdd BLAST977
Alternative sequenceiVSP_041929518 – 541MASTL…ASNKV → LPPANSSFMLPPTSFSSNYF HFLP in isoform 4. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_041930542 – 1338Missing in isoform 4. 1 PublicationAdd BLAST797
Alternative sequenceiVSP_002955657 – 687DQEAP…HANGV → GEHCNKKAVFSRISKFKSTR NDCTTQSNVKH in isoform 2. 3 PublicationsAdd BLAST31
Alternative sequenceiVSP_002956688 – 1338Missing in isoform 2. 3 PublicationsAdd BLAST651
Alternative sequenceiVSP_041927706 – 733GIILG…YHCKA → ELYTSTSPSSSSSSPLSSSS SSSSSSSS in isoform 3. 3 PublicationsAdd BLAST28
Alternative sequenceiVSP_041928734 – 1338Missing in isoform 3. 3 PublicationsAdd BLAST605

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51602 mRNA. Translation: CAA35946.1.
U01134 mRNA. Translation: AAC50060.1.
AF063657 mRNA. Translation: AAC16449.2.
EU826561 mRNA. Translation: ACF47597.1.
EU368830 mRNA. Translation: ACA62948.1.
DQ836394 mRNA. Translation: ABI53803.1.
DQ836395 mRNA. Translation: ABI53804.1.
DQ836396 mRNA. Translation: ABI53805.1.
EF491868 mRNA. Translation: ABS32268.1.
EF491869 mRNA. Translation: ABS32269.1.
EF491870 mRNA. Translation: ABS32270.1.
EU360600 mRNA. Translation: ACB05747.1.
EU332841 Genomic DNA. Translation: ABY87530.1.
AK292936 mRNA. Translation: BAF85625.1.
AK300392 mRNA. Translation: BAG62125.1.
AL138712, AL139005 Genomic DNA. Translation: CAI14846.1.
AL139005, AL138712 Genomic DNA. Translation: CAI17096.1.
CH471075 Genomic DNA. Translation: EAX08431.1.
CH471075 Genomic DNA. Translation: EAX08432.1.
BC039007 mRNA. Translation: AAH39007.1.
D00133 Genomic DNA. Translation: BAA00080.1.
CCDSiCCDS53860.1. [P17948-3]
CCDS53861.1. [P17948-4]
CCDS73556.1. [P17948-2]
CCDS9330.1. [P17948-1]
PIRiA49636.
S09982.
RefSeqiNP_001153392.1. NM_001159920.1. [P17948-2]
NP_001153502.1. NM_001160030.1. [P17948-3]
NP_001153503.1. NM_001160031.1. [P17948-4]
NP_002010.2. NM_002019.4. [P17948-1]
UniGeneiHs.594454.

Genome annotation databases

EnsembliENST00000282397; ENSP00000282397; ENSG00000102755. [P17948-1]
ENST00000539099; ENSP00000442630; ENSG00000102755. [P17948-4]
ENST00000541932; ENSP00000437631; ENSG00000102755. [P17948-3]
ENST00000543394; ENSP00000437841; ENSG00000102755. [P17948-8]
ENST00000615840; ENSP00000484039; ENSG00000102755. [P17948-2]
GeneIDi2321.
KEGGihsa:2321.
UCSCiuc001usb.4. human. [P17948-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51602 mRNA. Translation: CAA35946.1.
U01134 mRNA. Translation: AAC50060.1.
AF063657 mRNA. Translation: AAC16449.2.
EU826561 mRNA. Translation: ACF47597.1.
EU368830 mRNA. Translation: ACA62948.1.
DQ836394 mRNA. Translation: ABI53803.1.
DQ836395 mRNA. Translation: ABI53804.1.
DQ836396 mRNA. Translation: ABI53805.1.
EF491868 mRNA. Translation: ABS32268.1.
EF491869 mRNA. Translation: ABS32269.1.
EF491870 mRNA. Translation: ABS32270.1.
EU360600 mRNA. Translation: ACB05747.1.
EU332841 Genomic DNA. Translation: ABY87530.1.
AK292936 mRNA. Translation: BAF85625.1.
AK300392 mRNA. Translation: BAG62125.1.
AL138712, AL139005 Genomic DNA. Translation: CAI14846.1.
AL139005, AL138712 Genomic DNA. Translation: CAI17096.1.
CH471075 Genomic DNA. Translation: EAX08431.1.
CH471075 Genomic DNA. Translation: EAX08432.1.
BC039007 mRNA. Translation: AAH39007.1.
D00133 Genomic DNA. Translation: BAA00080.1.
CCDSiCCDS53860.1. [P17948-3]
CCDS53861.1. [P17948-4]
CCDS73556.1. [P17948-2]
CCDS9330.1. [P17948-1]
PIRiA49636.
S09982.
RefSeqiNP_001153392.1. NM_001159920.1. [P17948-2]
NP_001153502.1. NM_001160030.1. [P17948-3]
NP_001153503.1. NM_001160031.1. [P17948-4]
NP_002010.2. NM_002019.4. [P17948-1]
UniGeneiHs.594454.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FLTX-ray1.70X/Y132-226[»]
1QSVNMR-A129-229[»]
1QSZNMR-A129-229[»]
1QTYX-ray2.70T/U/X/Y129-229[»]
1RV6X-ray2.45X/Y130-229[»]
2XACX-ray2.71C/X129-226[»]
3HNGX-ray2.70A801-1158[»]
4CKVX-ray2.06X132-225[»]
4CL7X-ray2.00A/B/C/D132-225[»]
5ABDX-ray2.00E/I/X132-226[»]
5EX3X-ray2.41D827-835[»]
ProteinModelPortaliP17948.
SMRiP17948.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108609. 13 interactors.
DIPiDIP-643N.
IntActiP17948. 30 interactors.
MINTiMINT-127610.
STRINGi9606.ENSP00000282397.

Chemistry databases

BindingDBiP17948.
ChEMBLiCHEMBL1868.
DrugBankiDB06626. Axitinib.
DB09078. Lenvatinib.
DB09079. Nintedanib.
DB06589. Pazopanib.
DB08896. Regorafenib.
DB00398. Sorafenib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGYi1812.

PTM databases

iPTMnetiP17948.
PhosphoSitePlusiP17948.
UniCarbKBiP17948.

Polymorphism and mutation databases

BioMutaiFLT1.
DMDMi143811474.

Proteomic databases

EPDiP17948.
MaxQBiP17948.
PaxDbiP17948.
PeptideAtlasiP17948.
PRIDEiP17948.

Protocols and materials databases

DNASUi2321.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282397; ENSP00000282397; ENSG00000102755. [P17948-1]
ENST00000539099; ENSP00000442630; ENSG00000102755. [P17948-4]
ENST00000541932; ENSP00000437631; ENSG00000102755. [P17948-3]
ENST00000543394; ENSP00000437841; ENSG00000102755. [P17948-8]
ENST00000615840; ENSP00000484039; ENSG00000102755. [P17948-2]
GeneIDi2321.
KEGGihsa:2321.
UCSCiuc001usb.4. human. [P17948-1]

Organism-specific databases

CTDi2321.
DisGeNETi2321.
GeneCardsiFLT1.
H-InvDBHIX0130593.
HGNCiHGNC:3763. FLT1.
HPAiCAB068189.
CAB068190.
HPA011740.
HPA014290.
MIMi165070. gene.
neXtProtiNX_P17948.
OpenTargetsiENSG00000102755.
PharmGKBiPA28180.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP17948.
KOiK05096.
OMAiILTHIGH.
OrthoDBiEOG091G01TL.
PhylomeDBiP17948.
TreeFamiTF325768.

Enzyme and pathway databases

BioCyciZFISH:HS02408-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-194306. Neurophilin interactions with VEGF and VEGFR.
R-HSA-195399. VEGF binds to VEGFR leading to receptor dimerization.
SignaLinkiP17948.
SIGNORiP17948.

Miscellaneous databases

ChiTaRSiFLT1. human.
EvolutionaryTraceiP17948.
GeneWikiiFLT1.
GenomeRNAii2321.
PROiP17948.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102755.
CleanExiHS_FLT1.
ExpressionAtlasiP17948. baseline and differential.
GenevisibleiP17948. HS.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR001824. Tyr_kinase_rcpt_3_CS.
IPR009135. VEGFR1_rcpt.
[Graphical view]
PfamiPF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01833. VEGFRECEPTR1.
SMARTiSM00409. IG. 7 hits.
SM00408. IGc2. 5 hits.
SM00406. IGv. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 8 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 6 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVGFR1_HUMAN
AccessioniPrimary (citable) accession number: P17948
Secondary accession number(s): A3E342
, A3E344, A8KA71, B0LPF1, B2BF46, B2BF47, B2BF48, B3FR89, B5A923, F5H5L6, O60722, P16057, Q12954
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 3, 2007
Last modified: November 30, 2016
This is version 202 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.