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P17948 (VGFR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vascular endothelial growth factor receptor 1

Short name=VEGFR-1
EC=2.7.10.1
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 names
Name:FLT1
Synonyms:FLT, FRT, VEGFR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.2 Ref.4 Ref.5 Ref.6 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.34

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.14 Ref.15 Ref.17 Ref.22 Ref.24

Enzyme 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.

Subunit structure

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. Ref.2 Ref.3 Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.22 Ref.24 Ref.25 Ref.32 Ref.33 Ref.43 Ref.45

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein. Endosome. Note: Autophosphorylation promotes ubiquitination and endocytosis. Ref.2 Ref.4 Ref.5 Ref.20 Ref.25

Isoform 2: Secreted Ref.2 Ref.4 Ref.5 Ref.20 Ref.25.

Isoform 3: Secreted Ref.2 Ref.4 Ref.5 Ref.20 Ref.25.

Isoform 4: Secreted Ref.2 Ref.4 Ref.5 Ref.20 Ref.25.

Isoform 5: Cytoplasm Potential Ref.2 Ref.4 Ref.5 Ref.20 Ref.25.

Isoform 6: Cytoplasm Potential Ref.2 Ref.4 Ref.5 Ref.20 Ref.25.

Isoform 7: Cytoplasm Potential Ref.2 Ref.4 Ref.5 Ref.20 Ref.25.

Tissue specificity

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). Ref.5 Ref.6

Induction

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). Ref.5 Ref.16 Ref.34

Domain

The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFA binding. Ref.42 Ref.45

Post-translational modification

N-glycosylated. Ref.3 Ref.20

Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation. Ref.25

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. Ref.14 Ref.15 Ref.17 Ref.18 Ref.20 Ref.22 Ref.24 Ref.25 Ref.29 Ref.33

Involvement in disease

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.

Contains 7 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAngiogenesis
Chemotaxis
Differentiation
   Cellular componentCell membrane
Cytoplasm
Endosome
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cell migration

Inferred from mutant phenotype Ref.16. Source: UniProtKB

cellular response to vascular endothelial growth factor stimulus

Inferred from direct assay Ref.16. Source: UniProtKB

embryonic morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

monocyte chemotaxis

Inferred from direct assay Ref.29Ref.16. Source: UniProtKB

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.20Ref.17. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay Ref.17. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from direct assay Ref.17. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype Ref.23. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement PubMed 10748050. Source: ProtInc

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype Ref.22. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype Ref.23. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from mutant phenotype Ref.22. Source: UniProtKB

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay PubMed 1312256. Source: BHF-UCL

protein autophosphorylation

Inferred from direct assay Ref.20Ref.17. Source: UniProtKB

sprouting angiogenesis

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement Ref.1. Source: ProtInc

vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay Ref.17. Source: UniProtKB

vascular endothelial growth factor receptor-1 signaling pathway

Inferred from direct assay PubMed 15952180. Source: UniProtKB

   Cellular_componentendosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Traceable author statement Ref.2. Source: ProtInc

integral component of plasma membrane

Inferred from direct assay Ref.20. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

VEGF-A-activated receptor activity

Inferred from direct assay Ref.16. Source: UniProtKB

VEGF-B-activated receptor activity

Inferred from direct assay PubMed 15952180. Source: UniProtKB

growth factor binding

Inferred from physical interaction Ref.3Ref.20PubMed 12366396PubMed 16109918. Source: UniProtKB

placental growth factor-activated receptor activity

Inferred from direct assay Ref.24. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.43PubMed 12771128PubMed 1312256Ref.44PubMed 16893970PubMed 18273061PubMed 20660291PubMed 23397142PubMed 7657594Ref.42. Source: IntAct

transmembrane receptor protein tyrosine kinase activity

Traceable author statement Ref.2. Source: ProtInc

vascular endothelial growth factor-activated receptor activity

Inferred from direct assay Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P17948-1)

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.
Isoform 2 (identifier: P17948-2)

Also known as: sFlt1;

The sequence of this isoform differs from the canonical sequence as follows:
     657-687: DQEAPYLLRNLSDHTVAISSSTTLDCHANGV → GEHCNKKAVFSRISKFKSTRNDCTTQSNVKH
     688-1338: Missing.
Isoform 3 (identifier: P17948-3)

Also known as: sFlt1-14;

The sequence of this isoform differs from the canonical sequence as follows:
     706-733: GIILGPGSSTLFIERVTEEDEGVYHCKA → ELYTSTSPSSSSSSPLSSSSSSSSSSSS
     734-1338: Missing.
Isoform 4 (identifier: P17948-4)

The sequence of this isoform differs from the canonical sequence as follows:
     518-541: MASTLVVADSRISGIYICIASNKV → LPPANSSFMLPPTSFSSNYFHFLP
     542-1338: Missing.
Isoform 5 (identifier: P17948-5)

Also known as: i15;

The sequence of this isoform differs from the canonical sequence as follows:
     1-782: Missing.
Isoform 6 (identifier: P17948-6)

Also known as: i18;

The sequence of this isoform differs from the canonical sequence as follows:
     1-875: Missing.
Isoform 7 (identifier: P17948-7)

Also known as: i21;

The sequence of this isoform differs from the canonical sequence as follows:
     1-995: Missing.
Isoform 8 (identifier: P17948-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2
Chain27 – 13381312Vascular endothelial growth factor receptor 1
PRO_0000016768

Regions

Topological domain27 – 758732Extracellular Potential
Transmembrane759 – 78022Helical; Potential
Topological domain781 – 1338558Cytoplasmic Potential
Domain32 – 12392Ig-like C2-type 1
Domain151 – 21464Ig-like C2-type 2
Domain230 – 32798Ig-like C2-type 3
Domain335 – 42187Ig-like C2-type 4
Domain428 – 553126Ig-like C2-type 5
Domain556 – 65499Ig-like C2-type 6
Domain661 – 74787Ig-like C2-type 7
Domain827 – 1158332Protein kinase
Nucleotide binding833 – 8419ATP By similarity

Sites

Active site10221Proton acceptor By similarity
Binding site8611ATP By similarity
Site767 – 7682Cleavage; by PSEN1 Probable

Amino acid modifications

Modified residue9141Phosphotyrosine; by autocatalysis Probable
Modified residue10531Phosphotyrosine; by autocatalysis By similarity
Modified residue11691Phosphotyrosine; by autocatalysis Ref.17
Modified residue12131Phosphotyrosine; by autocatalysis Ref.14 Ref.17 Ref.18 Ref.20 Ref.24
Modified residue12421Phosphotyrosine; by autocatalysis Ref.14
Modified residue13091Phosphotyrosine; by autocatalysis Ref.24
Modified residue13271Phosphotyrosine; by autocatalysis Ref.14 Ref.24
Modified residue13331Phosphotyrosine; by autocatalysis Ref.14
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4171N-linked (GlcNAc...) Potential
Glycosylation4741N-linked (GlcNAc...) Potential
Glycosylation5471N-linked (GlcNAc...) Potential
Glycosylation5971N-linked (GlcNAc...) Potential
Glycosylation6201N-linked (GlcNAc...) Potential
Glycosylation6251N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 107 By similarity
Disulfide bond158 ↔ 207
Disulfide bond252 ↔ 311 By similarity
Disulfide bond454 ↔ 535 By similarity
Disulfide bond577 ↔ 636 By similarity
Disulfide bond682 ↔ 731 By similarity

Natural variations

Alternative sequence1 – 995995Missing in isoform 7.
VSP_041983
Alternative sequence1 – 875875Missing in isoform 6.
VSP_041984
Alternative sequence1 – 782782Missing in isoform 5.
VSP_041985
Alternative sequence1 – 77MVSYWDT → MNSDLLV in isoform 8.
VSP_047759
Alternative sequence8 – 984977Missing in isoform 8.
VSP_047760
Alternative sequence518 – 54124MASTL…ASNKV → LPPANSSFMLPPTSFSSNYF HFLP in isoform 4.
VSP_041929
Alternative sequence542 – 1338797Missing in isoform 4.
VSP_041930
Alternative sequence657 – 68731DQEAP…HANGV → GEHCNKKAVFSRISKFKSTR NDCTTQSNVKH in isoform 2.
VSP_002955
Alternative sequence688 – 1338651Missing in isoform 2.
VSP_002956
Alternative sequence706 – 73328GIILG…YHCKA → ELYTSTSPSSSSSSPLSSSS SSSSSSSS in isoform 3.
VSP_041927
Alternative sequence734 – 1338605Missing in isoform 3.
VSP_041928
Natural variant601K → T. Ref.46
Corresponds to variant rs56409818 [ dbSNP | Ensembl ].
VAR_042045
Natural variant1281I → L.
Corresponds to variant rs35073261 [ dbSNP | Ensembl ].
VAR_049719
Natural variant1441E → K. Ref.46
Corresponds to variant rs55974987 [ dbSNP | Ensembl ].
VAR_042046
Natural variant2811R → Q. Ref.46
Corresponds to variant rs55687105 [ dbSNP | Ensembl ].
VAR_042047
Natural variant4221L → I in a lung adenocarcinoma sample; somatic mutation. Ref.46
VAR_042048
Natural variant7811R → Q in a glioma low grade oligodendroglioma sample; somatic mutation. Ref.46
VAR_042049
Natural variant9381M → V. Ref.46
Corresponds to variant rs35549791 [ dbSNP | Ensembl ].
VAR_042050
Natural variant9821E → A. Ref.46
Corresponds to variant rs35832528 [ dbSNP | Ensembl ].
VAR_042051
Natural variant10611L → V in a bladder transitional cell carcinoma sample; somatic mutation. Ref.46
VAR_042052

Experimental info

Mutagenesis7671V → A: Abolishes proteolytic cleavage by PSEN1. Ref.33
Mutagenesis8611K → M: Abolishes enzyme activity. Abolishes interaction with PLCG. Ref.17
Mutagenesis9141Y → F: Reduces phosphorylation at other tyrosine residues. Ref.14
Mutagenesis10501N → D: Strongly increases kinase activity. Increases activity in promoting proliferation of endothelial cells. Ref.28
Mutagenesis11691Y → F: Loss of phosphorylation site. Abolishes interaction with PLCG. Ref.17
Mutagenesis12131Y → F: Loss of phosphorylation site. Abolishes interaction with PIK3R1. Ref.14
Mutagenesis12421Y → F: Loss of phosphorylation site. Ref.14
Mutagenesis13271Y → F: Loss of phosphorylation site. Ref.14
Mutagenesis13331Y → F: Loss of phosphorylation site. Abolishes interaction with CBL. Ref.14 Ref.25
Sequence conflict4901F → S in AAC16449. Ref.3
Sequence conflict7791F → L in CAA35946. Ref.1
Sequence conflict10291L → F in ABI53803. Ref.6
Sequence conflict10291L → F in ABI53804. Ref.6

Secondary structure

................................................................................. 1338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Flt1) [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: FF3381EEFAF0787C

FASTA1,338150,769
        10         20         30         40         50         60 
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH LQCRGEAAHK 

        70         80         90        100        110        120 
WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN HTGFYSCKYL AVPTSKKKET 

       130        140        150        160        170        180 
ESAIYIFISD TGRPFVEMYS EIPEIIHMTE GRELVIPCRV TSPNITVTLK KFPLDTLIPD 

       190        200        210        220        230        240 
GKRIIWDSRK GFIISNATYK EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV 

       250        260        270        280        290        300 
KLLRGHTLVL NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK 

       310        320        330        340        350        360 
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK RSYRLSMKVK 

       370        380        390        400        410        420 
AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA GNYTILLSIK QSNVFKNLTA 

       430        440        450        460        470        480 
TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ ILTCTAYGIP QPTIKWFWHP CNHNHSEARC 

       490        500        510        520        530        540 
DFCSNNEESF ILDADSNMGN RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK 

       550        560        570        580        590        600 
VGTVGRNISF YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM 

       610        620        630        640        650        660 
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK KEITIRDQEA 

       670        680        690        700        710        720 
PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK IQQEPGIILG PGSSTLFIER 

       730        740        750        760        770        780 
VTEEDEGVYH CKATNQKGSV ESSAYLTVQG TSDKSNLELI TLTCTCVAAT LFWLLLTLFI 

       790        800        810        820        830        840 
RKMKRSSSEI KTDYLSIIMD PDEVPLDEQC ERLPYDASKW EFARERLKLG KSLGRGAFGK 

       850        860        870        880        890        900 
VVQASAFGIK KSPTCRTVAV KMLKEGATAS EYKALMTELK ILTHIGHHLN VVNLLGACTK 

       910        920        930        940        950        960 
QGGPLMVIVE YCKYGNLSNY LKSKRDLFFL NKDAALHMEP KKEKMEPGLE QGKKPRLDSV 

       970        980        990       1000       1010       1020 
TSSESFASSG FQEDKSLSDV EEEEDSDGFY KEPITMEDLI SYSFQVARGM EFLSSRKCIH 

      1030       1040       1050       1060       1070       1080 
RDLAARNILL SENNVVKICD FGLARDIYKN PDYVRKGDTR LPLKWMAPES IFDKIYSTKS 

      1090       1100       1110       1120       1130       1140 
DVWSYGVLLW EIFSLGGSPY PGVQMDEDFC SRLREGMRMR APEYSTPEIY QIMLDCWHRD 

      1150       1160       1170       1180       1190       1200 
PKERPRFAEL VEKLGDLLQA NVQQDGKDYI PINAILTGNS GFTYSTPAFS EDFFKESISA 

      1210       1220       1230       1240       1250       1260 
PKFNSGSSDD VRYVNAFKFM SLERIKTFEE LLPNATSMFD DYQGDSSTLL ASPMLKRFTW 

      1270       1280       1290       1300       1310       1320 
TDSKPKASLK IDLRVTSKSK ESGLSDVSRP SFCHSSCGHV SEGKRRFTYD HAELERKIAC 

      1330 
CSPPPDYNSV VLYSTPPI 

« Hide

Isoform 2 (sFlt1) [UniParc].

Checksum: 3F73F4942469DA36
Show »

FASTA68777,474
Isoform 3 (sFlt1-14) [UniParc].

Checksum: 67B7F8BC1D30CD9E
Show »

FASTA73382,124
Isoform 4 [UniParc].

Checksum: 50BCDAACB69B0EA2
Show »

FASTA54160,917
Isoform 5 (i15) [UniParc].

Checksum: 9150507FBDF43B24
Show »

FASTA55662,954
Isoform 6 (i18) [UniParc].

Checksum: 7D3D572623A1124E
Show »

FASTA46352,613
Isoform 7 (i21) [UniParc].

Checksum: B7800AF7311BF0D6
Show »

FASTA34339,148
Isoform 8 [UniParc].

Checksum: 34E2B38DE128BA53
Show »

FASTA36141,175

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Role of PlGF in the intra- and intermolecular cross talk between the VEGF receptors Flt1 and Flk1."
Autiero M., Waltenberger J., Communi D., Kranz A., Moons L., Lambrechts D., Kroll J., Plaisance S., De Mol M., Bono F., Kliche S., Fellbrich G., Ballmer-Hofer K., Maglione D., Mayr-Beyrle U., Dewerchin M., Dombrowski S., Stanimirovic D. expand/collapse author list , Van Hummelen P., Dehio C., Hicklin D.J., Persico G., Herbert J.M., Communi D., Shibuya M., Collen D., Conway E.M., Carmeliet P.
Nat. Med. 9:936-943(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS53860.1. [P17948-3]
CCDS53861.1. [P17948-4]
CCDS9330.1. [P17948-1]
PIRA49636.
S09982.
RefSeqNP_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]
UniGeneHs.594454.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP17948.
SMRP17948. Positions 32-750, 787-1196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108609. 11 interactions.
DIPDIP-643N.
IntActP17948. 26 interactions.
MINTMINT-127610.
STRING9606.ENSP00000282397.

Chemistry

BindingDBP17948.
ChEMBLCHEMBL1868.
DrugBankDB01268. Sunitinib.
GuidetoPHARMACOLOGY1812.

PTM databases

PhosphoSiteP17948.

Polymorphism databases

DMDM143811474.

Proteomic databases

PaxDbP17948.
PRIDEP17948.

Protocols and materials databases

DNASU2321.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000282397; ENSP00000282397; ENSG00000102755. [P17948-1]
ENST00000539099; ENSP00000442630; ENSG00000102755. [P17948-4]
ENST00000540678; ENSP00000443311; ENSG00000102755. [P17948-5]
ENST00000541932; ENSP00000437631; ENSG00000102755. [P17948-3]
ENST00000543394; ENSP00000437841; ENSG00000102755. [P17948-8]
GeneID2321.
KEGGhsa:2321.
UCSCuc001usa.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

CTD2321.
GeneCardsGC13M028874.
H-InvDBHIX0130593.
HGNCHGNC:3763. FLT1.
HPAHPA011740.
HPA014290.
MIM165070. gene.
neXtProtNX_P17948.
PharmGKBPA28180.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000037949.
HOVERGENHBG053432.
InParanoidP17948.
KOK05096.
OMAKWEFARE.
OrthoDBEOG75F4CC.
PhylomeDBP17948.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkP17948.

Gene expression databases

ArrayExpressP17948.
BgeeP17948.
CleanExHS_FLT1.
GenevestigatorP17948.

Family and domain databases

Gene3D2.60.40.10. 7 hits.
InterProIPR007110. 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]
PANTHERPTHR24416:SF126. PTHR24416:SF126. 1 hit.
PfamPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR01833. VEGFRECEPTR1.
SMARTSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP17948.
GeneWikiFLT1.
GenomeRNAi2321.
NextBio35467213.
PROP17948.
SOURCESearch...

Entry information

Entry nameVGFR1_HUMAN
AccessionPrimary (citable) accession number: P17948
Secondary accession number(s): A3E342 expand/collapse secondary AC list , A3E344, A8KA71, B0LPF1, B2BF46, B2BF47, B2BF48, B3FR89, B5A923, F5H5L6, O60722, P16057, Q12954
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM