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P17948

- VGFR1_HUMAN

UniProt

P17948 - VGFR1_HUMAN

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Protein
Vascular endothelial growth factor receptor 1
Gene
FLT1, FLT, FRT, VEGFR1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.5 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei767 – 7682Cleavage; by PSEN1 Inferred
Binding sitei861 – 8611ATP By similarity
Active sitei1022 – 10221Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi833 – 8419ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. VEGF-A-activated receptor activity Source: UniProtKB
  3. VEGF-B-activated receptor activity Source: UniProtKB
  4. growth factor binding Source: UniProtKB
  5. placental growth factor-activated receptor activity Source: UniProtKB
  6. protein binding Source: IntAct
  7. transmembrane receptor protein tyrosine kinase activity Source: ProtInc
  8. vascular endothelial growth factor-activated receptor activity Source: UniProtKB

GO - Biological processi

  1. blood vessel morphogenesis Source: UniProtKB
  2. cell differentiation Source: UniProtKB-KW
  3. cell migration Source: UniProtKB
  4. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  5. embryonic morphogenesis Source: UniProtKB
  6. monocyte chemotaxis Source: UniProtKB
  7. patterning of blood vessels Source: Ensembl
  8. peptidyl-tyrosine phosphorylation Source: UniProtKB
  9. positive regulation of MAP kinase activity Source: UniProtKB
  10. positive regulation of MAPK cascade Source: UniProtKB
  11. positive regulation of angiogenesis Source: UniProtKB
  12. positive regulation of cell migration Source: UniProtKB
  13. positive regulation of cell proliferation Source: ProtInc
  14. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  15. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  16. positive regulation of phospholipase C activity Source: UniProtKB
  17. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  18. protein autophosphorylation Source: UniProtKB
  19. sprouting angiogenesis Source: Ensembl
  20. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
  21. vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  22. vascular endothelial growth factor receptor-1 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

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_12473. Neurophilin interactions with VEGF and VEGFR.
REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
SignaLinkiP17948.

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
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:3763. FLT1.

Subcellular locationi

Isoform 1 : Cell membrane; Single-pass type I membrane protein. Endosome
Note: Autophosphorylation promotes ubiquitination and endocytosis.5 Publications
Isoform 2 : Secreted 5 Publications
Isoform 3 : Secreted 5 Publications
Isoform 4 : Secreted 5 Publications
Isoform 5 : Cytoplasm Reviewed prediction 5 Publications
Isoform 6 : Cytoplasm Reviewed prediction 5 Publications
Isoform 7 : Cytoplasm Reviewed prediction 5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 758732Extracellular Reviewed prediction
Add
BLAST
Transmembranei759 – 78022Helical; Reviewed prediction
Add
BLAST
Topological domaini781 – 1338558Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endosome Source: UniProtKB-SubCell
  2. extracellular space Source: ProtInc
  3. integral component of plasma membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
  5. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi767 – 7671V → A: Abolishes proteolytic cleavage by PSEN1. 1 Publication
Mutagenesisi861 – 8611K → M: Abolishes enzyme activity. Abolishes interaction with PLCG. 1 Publication
Mutagenesisi914 – 9141Y → F: Reduces phosphorylation at other tyrosine residues. 1 Publication
Mutagenesisi1050 – 10501N → D: Strongly increases kinase activity. Increases activity in promoting proliferation of endothelial cells. 1 Publication
Mutagenesisi1169 – 11691Y → F: Loss of phosphorylation site. Abolishes interaction with PLCG. 1 Publication
Mutagenesisi1213 – 12131Y → F: Loss of phosphorylation site. Abolishes interaction with PIK3R1. 1 Publication
Mutagenesisi1242 – 12421Y → F: Loss of phosphorylation site. 1 Publication
Mutagenesisi1327 – 13271Y → F: Loss of phosphorylation site. 1 Publication
Mutagenesisi1333 – 13331Y → F: Loss of phosphorylation site. Abolishes interaction with CBL. 2 Publications

Organism-specific databases

PharmGKBiPA28180.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 Publication
Add
BLAST
Chaini27 – 13381312Vascular endothelial growth factor receptor 1
PRO_0000016768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 107 By similarity
Glycosylationi100 – 1001N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi158 ↔ 207
Glycosylationi164 – 1641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi196 – 1961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi251 – 2511N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi252 ↔ 311 By similarity
Glycosylationi323 – 3231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi402 – 4021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi417 – 4171N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi454 ↔ 535 By similarity
Glycosylationi474 – 4741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi547 – 5471N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi577 ↔ 636 By similarity
Glycosylationi597 – 5971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi620 – 6201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi625 – 6251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi666 – 6661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi682 ↔ 731 By similarity
Modified residuei914 – 9141Phosphotyrosine; by autocatalysis Inferred
Modified residuei1053 – 10531Phosphotyrosine; by autocatalysis By similarity
Modified residuei1169 – 11691Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1213 – 12131Phosphotyrosine; by autocatalysis5 Publications
Modified residuei1242 – 12421Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1309 – 13091Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1327 – 13271Phosphotyrosine; by autocatalysis2 Publications
Modified residuei1333 – 13331Phosphotyrosine; by autocatalysis1 Publication

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.10 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP17948.
PRIDEiP17948.

PTM databases

PhosphoSiteiP17948.

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).3 Publications

Gene expression databases

ArrayExpressiP17948.
BgeeiP17948.
CleanExiHS_FLT1.
GenevestigatoriP17948.

Organism-specific databases

HPAiHPA011740.
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 GNB2L1/RACK1. Identified in a complex with CBL and CD2AP.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBLP226812EBI-1026718,EBI-518228
CRKLP461099EBI-1026718,EBI-910
CTNNB1P352222EBI-1026718,EBI-491549
HCKP086312EBI-1026718,EBI-346340
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

Protein-protein interaction databases

BioGridi108609. 11 interactions.
DIPiDIP-643N.
IntActiP17948. 26 interactions.
MINTiMINT-127610.
STRINGi9606.ENSP00000282397.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni130 – 1323
Beta strandi135 – 1373
Beta strandi140 – 1423
Beta strandi144 – 1485
Beta strandi150 – 1523
Beta strandi154 – 1563
Beta strandi160 – 1623
Helixi163 – 1653
Beta strandi168 – 1714
Turni172 – 1743
Beta strandi175 – 1773
Beta strandi181 – 1877
Turni188 – 1903
Beta strandi191 – 1966
Helixi199 – 2013
Beta strandi203 – 2119
Beta strandi214 – 22411
Helixi806 – 8094
Helixi817 – 8204
Helixi824 – 8263
Beta strandi827 – 8359
Beta strandi837 – 84812
Helixi849 – 8513
Beta strandi854 – 86310
Helixi869 – 88315
Beta strandi894 – 8985
Beta strandi906 – 9105
Helixi917 – 9226
Helixi996 – 101419
Turni1015 – 10173
Helixi1025 – 10273
Beta strandi1028 – 10303
Helixi1032 – 10343
Beta strandi1036 – 10383
Helixi1042 – 10443
Turni1047 – 10493
Beta strandi1053 – 10553
Helixi1063 – 10653
Helixi1068 – 10736
Helixi1078 – 109316
Helixi1107 – 11137
Turni1114 – 11163
Helixi1127 – 113610
Helixi1141 – 11433
Helixi1147 – 115711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP17948.
SMRiP17948. Positions 32-750, 787-1196.

Miscellaneous databases

EvolutionaryTraceiP17948.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12392Ig-like C2-type 1
Add
BLAST
Domaini151 – 21464Ig-like C2-type 2
Add
BLAST
Domaini230 – 32798Ig-like C2-type 3
Add
BLAST
Domaini335 – 42187Ig-like C2-type 4
Add
BLAST
Domaini428 – 553126Ig-like C2-type 5
Add
BLAST
Domaini556 – 65499Ig-like C2-type 6
Add
BLAST
Domaini661 – 74787Ig-like C2-type 7
Add
BLAST
Domaini827 – 1158332Protein kinase
Add
BLAST

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP17948.
KOiK05096.
OMAiKWEFARE.
OrthoDBiEOG75F4CC.
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.
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]
PANTHERiPTHR24416:SF126. PTHR24416:SF126. 1 hit.
PfamiPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR01833. VEGFRECEPTR1.
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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. Align

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

MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH     50
LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN 100
HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE 150
GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK 200
EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL 250
NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK 300
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK 350
RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA 400
GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ 450
ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN 500
RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF 550
YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM 600
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK 650
KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK 700
IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG 750
TSDKSNLELI TLTCTCVAAT LFWLLLTLFI RKMKRSSSEI KTDYLSIIMD 800
PDEVPLDEQC ERLPYDASKW EFARERLKLG KSLGRGAFGK VVQASAFGIK 850
KSPTCRTVAV KMLKEGATAS EYKALMTELK ILTHIGHHLN VVNLLGACTK 900
QGGPLMVIVE YCKYGNLSNY LKSKRDLFFL NKDAALHMEP KKEKMEPGLE 950
QGKKPRLDSV TSSESFASSG FQEDKSLSDV EEEEDSDGFY KEPITMEDLI 1000
SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN 1050
PDYVRKGDTR LPLKWMAPES IFDKIYSTKS DVWSYGVLLW EIFSLGGSPY 1100
PGVQMDEDFC SRLREGMRMR APEYSTPEIY QIMLDCWHRD PKERPRFAEL 1150
VEKLGDLLQA NVQQDGKDYI PINAILTGNS GFTYSTPAFS EDFFKESISA 1200
PKFNSGSSDD VRYVNAFKFM SLERIKTFEE LLPNATSMFD DYQGDSSTLL 1250
ASPMLKRFTW TDSKPKASLK IDLRVTSKSK ESGLSDVSRP SFCHSSCGHV 1300
SEGKRRFTYD HAELERKIAC CSPPPDYNSV VLYSTPPI 1338
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601K → T.1 Publication
Corresponds to variant rs56409818 [ dbSNP | Ensembl ].
VAR_042045
Natural varianti128 – 1281I → L.
Corresponds to variant rs35073261 [ dbSNP | Ensembl ].
VAR_049719
Natural varianti144 – 1441E → K.1 Publication
Corresponds to variant rs55974987 [ dbSNP | Ensembl ].
VAR_042046
Natural varianti281 – 2811R → Q.1 Publication
Corresponds to variant rs55687105 [ dbSNP | Ensembl ].
VAR_042047
Natural varianti422 – 4221L → I in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042048
Natural varianti781 – 7811R → Q in a glioma low grade oligodendroglioma sample; somatic mutation. 1 Publication
VAR_042049
Natural varianti938 – 9381M → V.1 Publication
Corresponds to variant rs35549791 [ dbSNP | Ensembl ].
VAR_042050
Natural varianti982 – 9821E → A.1 Publication
Corresponds to variant rs35832528 [ dbSNP | Ensembl ].
VAR_042051
Natural varianti1061 – 10611L → V in a bladder transitional cell carcinoma sample; somatic mutation. 1 Publication
VAR_042052

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 995995Missing in isoform 7.
VSP_041983Add
BLAST
Alternative sequencei1 – 875875Missing in isoform 6.
VSP_041984Add
BLAST
Alternative sequencei1 – 782782Missing in isoform 5.
VSP_041985Add
BLAST
Alternative sequencei1 – 77MVSYWDT → MNSDLLV in isoform 8.
VSP_047759
Alternative sequencei8 – 984977Missing in isoform 8.
VSP_047760Add
BLAST
Alternative sequencei518 – 54124MASTL…ASNKV → LPPANSSFMLPPTSFSSNYF HFLP in isoform 4.
VSP_041929Add
BLAST
Alternative sequencei542 – 1338797Missing in isoform 4.
VSP_041930Add
BLAST
Alternative sequencei657 – 68731DQEAP…HANGV → GEHCNKKAVFSRISKFKSTR NDCTTQSNVKH in isoform 2.
VSP_002955Add
BLAST
Alternative sequencei688 – 1338651Missing in isoform 2.
VSP_002956Add
BLAST
Alternative sequencei706 – 73328GIILG…YHCKA → ELYTSTSPSSSSSSPLSSSS SSSSSSSS in isoform 3.
VSP_041927Add
BLAST
Alternative sequencei734 – 1338605Missing in isoform 3.
VSP_041928Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti490 – 4901F → S in AAC16449. 1 Publication
Sequence conflicti779 – 7791F → L in CAA35946. 1 Publication
Sequence conflicti1029 – 10291L → F in ABI53803. 1 Publication
Sequence conflicti1029 – 10291L → F in ABI53804. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
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]
ENST00000540678; ENSP00000443311; ENSG00000102755. [P17948-5]
ENST00000541932; ENSP00000437631; ENSG00000102755. [P17948-3]
ENST00000543394; ENSP00000437841; ENSG00000102755. [P17948-8]
GeneIDi2321.
KEGGihsa:2321.
UCSCiuc001usa.3. human. [P17948-5]
uc001usb.3. human. [P17948-1]
uc001usc.3. human. [P17948-2]
uc010aap.2. human. [P17948-7]
uc010aaq.2. human. [P17948-6]
uc010aar.1. human. [P17948-3]
uc010tdp.1. human. [P17948-4]

Polymorphism databases

DMDMi143811474.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53860.1. [P17948-3 ]
CCDS53861.1. [P17948-4 ]
CCDS9330.1. [P17948-1 ]
PIRi A49636.
S09982.
RefSeqi NP_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 ]
UniGenei Hs.594454.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FLT X-ray 1.70 X/Y 132-226 [» ]
1QSV NMR - A 129-229 [» ]
1QSZ NMR - A 129-229 [» ]
1QTY X-ray 2.70 T/U/X/Y 129-229 [» ]
1RV6 X-ray 2.45 X/Y 130-229 [» ]
2XAC X-ray 2.71 C/X 129-226 [» ]
3HNG X-ray 2.70 A 801-1158 [» ]
ProteinModelPortali P17948.
SMRi P17948. Positions 32-750, 787-1196.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108609. 11 interactions.
DIPi DIP-643N.
IntActi P17948. 26 interactions.
MINTi MINT-127610.
STRINGi 9606.ENSP00000282397.

Chemistry

BindingDBi P17948.
ChEMBLi CHEMBL1868.
DrugBanki DB01268. Sunitinib.
GuidetoPHARMACOLOGYi 1812.

PTM databases

PhosphoSitei P17948.

Polymorphism databases

DMDMi 143811474.

Proteomic databases

PaxDbi P17948.
PRIDEi P17948.

Protocols and materials databases

DNASUi 2321.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000282397 ; ENSP00000282397 ; ENSG00000102755 . [P17948-1 ]
ENST00000539099 ; ENSP00000442630 ; ENSG00000102755 . [P17948-4 ]
ENST00000540678 ; ENSP00000443311 ; ENSG00000102755 . [P17948-5 ]
ENST00000541932 ; ENSP00000437631 ; ENSG00000102755 . [P17948-3 ]
ENST00000543394 ; ENSP00000437841 ; ENSG00000102755 . [P17948-8 ]
GeneIDi 2321.
KEGGi hsa:2321.
UCSCi uc001usa.3. human. [P17948-5 ]
uc001usb.3. human. [P17948-1 ]
uc001usc.3. human. [P17948-2 ]
uc010aap.2. human. [P17948-7 ]
uc010aaq.2. human. [P17948-6 ]
uc010aar.1. human. [P17948-3 ]
uc010tdp.1. human. [P17948-4 ]

Organism-specific databases

CTDi 2321.
GeneCardsi GC13M028874.
H-InvDB HIX0130593.
HGNCi HGNC:3763. FLT1.
HPAi HPA011740.
HPA014290.
MIMi 165070. gene.
neXtProti NX_P17948.
PharmGKBi PA28180.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000037949.
HOVERGENi HBG053432.
InParanoidi P17948.
KOi K05096.
OMAi KWEFARE.
OrthoDBi EOG75F4CC.
PhylomeDBi P17948.
TreeFami TF325768.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 2681.
Reactomei REACT_12473. Neurophilin interactions with VEGF and VEGFR.
REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
SignaLinki P17948.

Miscellaneous databases

EvolutionaryTracei P17948.
GeneWikii FLT1.
GenomeRNAii 2321.
NextBioi 35467213.
PROi P17948.
SOURCEi Search...

Gene expression databases

ArrayExpressi P17948.
Bgeei P17948.
CleanExi HS_FLT1.
Genevestigatori P17948.

Family and domain databases

Gene3Di 2.60.40.10. 7 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
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 ]
PANTHERi PTHR24416:SF126. PTHR24416:SF126. 1 hit.
Pfami PF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PRINTSi PR01833. VEGFRECEPTR1.
SMARTi SM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50835. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family."
    Shibuya M., Yamaguchi S., Yamane A., Ikeda T., Tojo A., Matsushime H., Sato M.
    Oncogene 5:519-524(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor."
    Kendall R.L., Thomas K.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:10705-10709(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION (ISOFORM 2), INTERACTION WITH VEGFA, FUNCTION.
    Tissue: Umbilical vein.
  3. "Characterization of the VEGF binding site on the Flt-1 receptor."
    Herley M.T., Yu Y., Whitney R.G., Sato J.D.
    Biochem. Biophys. Res. Commun. 262:731-738(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH VEGFA, GLYCOSYLATION.
    Tissue: Umbilical vein.
  4. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
    Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
    Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION IN LIGAND BINDING, SUBCELLULAR LOCATION.
  5. "A novel human-specific soluble vascular endothelial growth factor receptor 1: cell-type-specific splicing and implications to vascular endothelial growth factor homeostasis and preeclampsia."
    Sela S., Itin A., Natanson-Yaron S., Greenfield C., Goldman-Wohl D., Yagel S., Keshet E.
    Circ. Res. 102:1566-1574(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ROLE IN PREECLAMPSIA, INDUCTION.
  6. "A novel intracellular isoform of VEGFR-1 activates Src and promotes cell invasion in MDA-MB-231 breast cancer cells."
    Mezquita B., Mezquita J., Pau M., Mezquita C.
    J. Cell. Biochem. 110:732-742(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6; 7 AND 8), ALTERNATIVE SPLICING, FUNCTION IN PHOSPHORYLATION OF SRC AND CANCER CELL INVASIVENESS, TISSUE SPECIFICITY.
  7. "A new VEGFR1 receptor transcript coding for the extracellular domains of the protein followed by a C-terminal polyserine tail."
    Mezquita J., Mezquita B., Pau M., Mezquita C.
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  8. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Placenta and Trachea.
  10. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Ovary.
  13. "A possible new member of tyrosine kinase family, human frt sequence, is highly conserved in vertebrates and located on human chromosome 13."
    Matsushime H., Yoshida M.C., Sasaki M., Shibuya M.
    Jpn. J. Cancer Res. 78:655-661(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1018-1058, ALTERNATIVE SPLICING (ISOFORM 1).
  14. "Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules."
    Ito N., Wernstedt C., Engstrom U., Claesson-Welsh L.
    J. Biol. Chem. 273:23410-23418(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, MUTAGENESIS OF TYR-914; TYR-1213; TYR-1242; TYR-1327 AND TYR-1333, INTERACTION WITH PLCG; GRB2; CRK; NCK1 AND PTPN11.
  15. "A unique signal transduction from FLT tyrosine kinase, a receptor for vascular endothelial growth factor VEGF."
    Seetharam L., Gotoh N., Maru Y., Neufeld G., Yamaguchi S., Shibuya M.
    Oncogene 10:135-147(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VEGFA, AUTOPHOSPHORYLATION, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF PLCG, ABSENCE OF MITOGENIC FUNCTION IN CULTURED FIBROBLASTS.
  16. "Migration of human monocytes in response to vascular endothelial growth factor (VEGF) is mediated via the VEGF receptor flt-1."
    Barleon B., Sozzani S., Zhou D., Weich H.A., Mantovani A., Marme D.
    Blood 87:3336-3343(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION, FUNCTION IN VEGFA AND PGF SIGNALING, INDUCTION.
  17. "The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-1) is a major binding site for PLCgamma."
    Sawano A., Takahashi T., Yamaguchi S., Shibuya M.
    Biochem. Biophys. Res. Commun. 238:487-491(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG AND ACTIVATION OF MAP KINASES, INTERACTION WITH PLCG, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-861 AND TYR-1169, PHOSPHORYLATION AT TYR-1169 AND TYR-1213.
  18. "Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
    Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
    Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3R1; PTPN11 AND NCK1, PHOSPHORYLATION AT TYR-1213.
  19. "Vascular endothelial growth factor receptor-2-mediated mitogenesis is negatively regulated by vascular endothelial growth factor receptor-1 in tumor epithelial cells."
    Dunk C., Ahmed A.
    Am. J. Pathol. 158:265-273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS NEGATIVE REGULATOR OF KDR-MEDIATED CELL PROLIFERATION.
  20. "Direct identification of a major autophosphorylation site on vascular endothelial growth factor receptor Flt-1 that mediates phosphatidylinositol 3'-kinase binding."
    Yu Y., Hulmes J.D., Herley M.T., Whitney R.G., Crabb J.W., Sato J.D.
    Biochem. J. 358:465-472(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3R1 AND VEGFA, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-1213, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION.
  21. "Effect of placenta growth factor-1 on proliferation and release of nitric oxide, cyclic AMP and cyclic GMP in human epithelial cells expressing the FLT-1 receptor."
    Angelucci C., Lama G., Iacopino F., Maglione D., Sica G.
    Growth Factors 19:193-206(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PGF-MEDIATED CHORIOCARCINOMA CELL PROLIFERATION.
  22. "Signaling properties of VEGF receptor-1 and -2 homo- and heterodimers."
    Huang K., Andersson C., Roomans G.M., Ito N., Claesson-Welsh L.
    Int. J. Biochem. Cell Biol. 33:315-324(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, FUNCTION IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG AND ACTIVATION OF PHOSPHATIDYLINOSITOL KINASE AND PHOSPHOLIPASE C.
  23. "Activation of vascular endothelial growth factor receptor-1 sustains angiogenesis and Bcl-2 expression via the phosphatidylinositol 3-kinase pathway in endothelial cells."
    Cai J., Ahmad S., Jiang W.G., Huang J., Kontos C.D., Boulton M., Ahmed A.
    Diabetes 52:2959-2968(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SIGNALING VIA ACTIVATION OF THE PHOSPHATIDYLINOSITOL KINASE PATHWAY AND POSITIVE REGULATION OF ANGIOGENESIS IN RESPONSE TO PGF AND VEGFA.
  24. Cited for: INTERACTION WITH PGF AND KDR, FUNCTION IN PHOSPHORYLATION OF KDR; VEGFA AND PGF SIGNALING, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-1213; TYR-1327 AND TYR-1309.
  25. "The c-Cbl/CD2AP complex regulates VEGF-induced endocytosis and degradation of Flt-1 (VEGFR-1)."
    Kobayashi S., Sawano A., Nojima Y., Shibuya M., Maru Y.
    FASEB J. 18:929-931(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL AND CD2AP, UBIQUITINATION, AUTOPHOSPHORYLATION IN RESPONSE TO VEGFA, MUTAGENESIS OF TYR-1333, SUBCELLULAR LOCATION.
  26. "Expression and function of vascular endothelial growth factor receptor-1 on human colorectal cancer cells."
    Fan F., Wey J.S., McCarty M.F., Belcheva A., Liu W., Bauer T.W., Somcio R.J., Wu Y., Hooper A., Hicklin D.J., Ellis L.M.
    Oncogene 24:2647-2653(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN VEGFA AND VEGFB SIGNALING; CANCER CELL MIGRATION; INVASIVENESS AND ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1.
  27. "Vascular endothelial growth factor receptor-1 mediates migration of human colorectal carcinoma cells by activation of Src family kinases."
    Lesslie D.P., Summy J.M., Parikh N.U., Fan F., Trevino J.G., Sawyer T.K., Metcalf C.A., Shakespeare W.C., Hicklin D.J., Ellis L.M., Gallick G.E.
    Br. J. Cancer 94:1710-1717(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL MIGRATION AND PHOSPHORYLATION OF PTK2/FAK1; YES1 AND SRC.
  28. "A single amino acid substitution in the activation loop defines the decoy characteristic of VEGFR-1/FLT-1."
    Meyer R.D., Mohammadi M., Rahimi N.
    J. Biol. Chem. 281:867-875(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-1050.
  29. "The molecular basis of VEGFR-1 signal transduction pathways in primary human monocytes."
    Tchaikovski V., Fellbrich G., Waltenberger J.
    Arterioscler. Thromb. Vasc. Biol. 28:322-328(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PGF AND VEGFA SIGNALING; PHOSPHORYLATION OF AKT1; MAPK3/ERK1 AND MAP KINASES; CHEMOTAXIS AND ACTIVATION OF PHOSPHATIDYLINOSITOL 3-KINASE, AUTOPHOSPHORYLATION IN RESPONSE TO PGF AND VEGFA.
  30. "Vascular endothelial growth factor receptor-1 regulates postnatal angiogenesis through inhibition of the excessive activation of Akt."
    Nishi J., Minamino T., Miyauchi H., Nojima A., Tateno K., Okada S., Orimo M., Moriya J., Fong G.H., Sunagawa K., Shibuya M., Komuro I.
    Circ. Res. 103:261-268(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOTHELIAL CELL SURVIVAL AND ANGIOGENESIS.
  31. "Placental growth factor (PlGF) enhances breast cancer cell motility by mobilising ERK1/2 phosphorylation and cytoskeletal rearrangement."
    Taylor A.P., Leon E., Goldenberg D.M.
    Br. J. Cancer 103:82-89(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CANCER CELL MIGRATION AND ACTIVATION OF MAPK1/ERK2 AND/OR MAPK3/ERK1.
  32. "RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3-K/Akt pathway."
    Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.
    J. Biol. Chem. 286:9097-9106(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GNB2L1.
  33. "gamma-Secretase and presenilin mediate cleavage and phosphorylation of vascular endothelial growth factor receptor-1."
    Cai J., Chen Z., Ruan Q., Han S., Liu L., Qi X., Boye S.L., Hauswirth W.W., Grant M.B., Boulton M.E.
    J. Biol. Chem. 286:42514-42523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSEN1 AND PTPRB, DEPHOSPHORYLATION BY PTPRB, MUTAGENESIS OF VAL-767, PROTEOLYTIC CLEAVAGE BY PSEN1 AT VAL-767.
  34. "Autocrine activity of soluble Flt-1 controls endothelial cell function and angiogenesis."
    Ahmad S., Hewett P.W., Al-Ani B., Sissaoui S., Fujisawa T., Cudmore M.J., Ahmed A.
    Vasc. Cell 3:15-15(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS DECOY RECEPTORS; REGULATION OF VEGFA SIGNALING AND REGULATION OF KDR ACTIVITY (ISOFORMS 2/3/4), ROLE IN PREECLAMPSIA.
  35. "Differential roles of vascular endothelial growth factor receptor-1 and receptor-2 in angiogenesis."
    Shibuya M.
    J. Biochem. Mol. Biol. 39:469-478(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION AS NEGATIVE REGULATOR OF ANGIOGENESIS DURING EMBRYONIC DEVELOPMENT; POSITIVE REGULATION OF MACROPHAGE FUNCTION IN ADULTHOOD; ROLE IN CARCINOGENESIS AND INFLAMMATION.
  36. "VEGF receptor protein-tyrosine kinases: structure and regulation."
    Roskoski R. Jr.
    Biochem. Biophys. Res. Commun. 375:287-291(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON STRUCTURE AND FUNCTION.
  37. "VEGFs and receptors involved in angiogenesis versus lymphangiogenesis."
    Lohela M., Bry M., Tammela T., Alitalo K.
    Curr. Opin. Cell Biol. 21:154-165(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
  38. "Structure-function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling."
    Grunewald F.S., Prota A.E., Giese A., Ballmer-Hofer K.
    Biochim. Biophys. Acta 1804:567-580(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND SIGNALING.
  39. "Vascular endothelial growth factor receptor-1 in human cancer: concise review and rationale for development of IMC-18F1 (Human antibody targeting vascular endothelial growth factor receptor-1)."
    Schwartz J.D., Rowinsky E.K., Youssoufian H., Pytowski B., Wu Y.
    Cancer 116:1027-1032(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN CANCER.
  40. "Signal transduction by vascular endothelial growth factor receptors."
    Koch S., Tugues S., Li X., Gualandi L., Claesson-Welsh L.
    Biochem. J. 437:169-183(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND SIGNALING.
  41. "Involvement of Flt-1 (VEGF receptor-1) in cancer and preeclampsia."
    Shibuya M.
    Proc. Jpn. Acad., B, Phys. Biol. Sci. 87:167-178(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN CANCER AND PREECLAMPSIA.
  42. "Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor."
    Wiesmann C., Fuh G., Christinger H.W., Eigenbrot C., Wells J.A., de Vos A.M.
    Cell 91:695-704(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 132-226 IN COMPLEX WITH VEGFA, DOMAIN.
  43. "Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states."
    Starovasnik M.A., Christinger H.W., Wiesmann C., Champe M.A., de Vos A.M., Skelton N.J.
    J. Mol. Biol. 293:531-544(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 129-229, X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 129-229 IN COMPLEX WITH VEGFA, SUBUNIT, INTERACTION WITH VEGFA.
  44. "The crystal structure of placental growth factor in complex with domain 2 of vascular endothelial growth factor receptor-1."
    Christinger H.W., Fuh G., de Vos A.M., Wiesmann C.
    J. Biol. Chem. 279:10382-10388(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 130-229 IN COMPLEX WITH PGF.
  45. "Structural insights into the binding of vascular endothelial growth factor-B by VEGFR-1(D2): recognition and specificity."
    Iyer S., Darley P.I., Acharya K.R.
    J. Biol. Chem. 285:23779-23789(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 129-226 IN COMPLEX WITH VEGFB, INTERACTION WITH VEGFB, SUBUNIT, DOMAIN.
  46. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-60; LYS-144; GLN-281; ILE-422; GLN-781; VAL-938; ALA-982 AND VAL-1061.

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: September 3, 2014
This is version 180 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

External Data

Dasty 3

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