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P35969

- VGFR1_MOUSE

UniProt

P35969 - VGFR1_MOUSE

Protein

Vascular endothelial growth factor receptor 1

Gene

Flt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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, and proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts. Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to the 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, YES1 and PLCG, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 and PTK2/FAK1 By similarity.By similarity

    Catalytic activityi

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

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei768 – 7692Cleavage; by PSEN1By similarity
    Binding sitei862 – 8621ATPPROSITE-ProRule annotation
    Active sitei1022 – 10221Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi834 – 8429ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: MGI
    3. placental growth factor-activated receptor activity Source: Ensembl
    4. vascular endothelial growth factor-activated receptor activity Source: MGI
    5. VEGF-A-activated receptor activity Source: Ensembl
    6. VEGF-B-activated receptor activity Source: Ensembl

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. blood vessel morphogenesis Source: UniProtKB
    3. cell differentiation Source: UniProtKB-KW
    4. cell migration Source: UniProtKB
    5. embryonic morphogenesis Source: UniProtKB
    6. monocyte chemotaxis Source: Ensembl
    7. patterning of blood vessels Source: MGI
    8. peptidyl-tyrosine phosphorylation Source: UniProtKB
    9. positive regulation of angiogenesis Source: Ensembl
    10. positive regulation of cell migration Source: Ensembl
    11. positive regulation of MAP kinase activity Source: Ensembl
    12. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
    13. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    14. positive regulation of phospholipase C activity Source: Ensembl
    15. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: Ensembl
    16. protein autophosphorylation Source: UniProtKB
    17. sprouting angiogenesis Source: MGI
    18. vascular endothelial growth factor receptor signaling pathway Source: MGI
    19. vascular endothelial growth factor signaling pathway Source: GOC

    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. 3474.
    ReactomeiREACT_205099. VEGF binds to VEGFR leading to receptor dimerization.
    REACT_227870. Neurophilin interactions with VEGF and VEGFR.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vascular endothelial growth factor receptor 1 (EC:2.7.10.1)
    Short name:
    VEGFR-1
    Alternative name(s):
    Embryonic receptor kinase 2
    Fms-like tyrosine kinase 1
    Short name:
    FLT-1
    Tyrosine-protein kinase receptor FLT
    Gene namesi
    Name:Flt1
    Synonyms:Emrk2, Flt, Vegfr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:95558. Flt1.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Endosome By similarity
    Note: Autophosphorylation promotes ubiquitination and endocytosis.By similarity

    GO - Cellular componenti

    1. endosome Source: UniProtKB-SubCell
    2. Golgi apparatus Source: Ensembl
    3. integral component of plasma membrane Source: UniProtKB
    4. nucleus Source: Ensembl
    5. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic lethality at about 9 dpc, due to defects in the formation and organization of the vascular network. Mice display abnormal blood island structures in the yolk sac, leading to defects in the organization of the vascular endothelium, excess growth and disorganization of embryonic and extraembryonic vasculature, including the endocardium and the microvasculature. Mice expressing a mutant protein that lacks the kinase domain survive and have no apparent phenotype.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 13331311Vascular endothelial growth factor receptor 1PRO_0000016769Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi53 ↔ 108PROSITE-ProRule annotation
    Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi159 ↔ 208PROSITE-ProRule annotation
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi253 ↔ 312PROSITE-ProRule annotation
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi455 ↔ 536PROSITE-ProRule annotation
    Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi517 – 5171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi578 ↔ 637PROSITE-ProRule annotation
    Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi667 – 6671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi683 ↔ 732PROSITE-ProRule annotation
    Glycosylationi714 – 7141N-linked (GlcNAc...)Sequence Analysis
    Modified residuei915 – 9151Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1053 – 10531Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1169 – 11691Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1213 – 12131Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1242 – 12421Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1322 – 13221Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1328 – 13281Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    N-glycosylated.By similarity
    Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation.By similarity
    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-1328 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP35969.
    PRIDEiP35969.

    PTM databases

    PhosphoSiteiP35969.

    Expressioni

    Gene expression databases

    ArrayExpressiP35969.
    BgeeiP35969.
    CleanExiMM_FLT1.
    GenevestigatoriP35969.

    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 (tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts with PTPRB. Interacts with GNB2L1/RACK1. Identified in a complex with CBL and CD2AP By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199706. 5 interactions.
    DIPiDIP-39359N.
    IntActiP35969. 8 interactions.
    MINTiMINT-4139959.

    Structurei

    3D structure databases

    ProteinModelPortaliP35969.
    SMRiP35969. Positions 32-751, 788-1197.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 759737ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini782 – 1333552CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei760 – 78122HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 12493Ig-like C2-type 1Add
    BLAST
    Domaini152 – 21564Ig-like C2-type 2Add
    BLAST
    Domaini231 – 32898Ig-like C2-type 3Add
    BLAST
    Domaini334 – 42996Ig-like C2-type 4Add
    BLAST
    Domaini430 – 550121Ig-like C2-type 5Add
    BLAST
    Domaini557 – 656100Ig-like C2-type 6Add
    BLAST
    Domaini662 – 74887Ig-like C2-type 7Add
    BLAST
    Domaini828 – 1158331Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

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

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108679.
    HOGENOMiHOG000037949.
    HOVERGENiHBG053432.
    InParanoidiP35969.
    KOiK05096.
    OrthoDBiEOG75F4CC.
    PhylomeDBiP35969.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 7 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR013106. Ig_V-set.
    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. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 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. 5 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]

    Sequencei

    Sequence statusi: Complete.

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

    P35969-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVSCWDTAVL PYALLGCLLL TGYGSGSKLK VPELSLKGTQ HVMQAGQTLF     50
    LKCRGEAAHS WSLPTTVSQE DKRLSITPPS ACGRDNRQFC STLTLDTAQA 100
    NHTGLYTCRY LPTSTSKKKK AESSIYIFVS DAGSPFIEMH TDIPKLVHMT 150
    EGRQLIIPCR VTSPNVTVTL KKFPFDTLTP DGQRITWDSR RGFIIANATY 200
    KEIGLLNCEA TVNGHLYQTN YLTHRQTNTI LDVQIRPPSP VRLLHGQTLV 250
    LNCTATTELN TRVQMSWNYP GKATKRASIR QRIDRSHSHN NVFHSVLKIN 300
    NVESRDKGLY TCRVKSGSSF QSFNTSVHVY EKGFISVKHR KQPVQETTAG 350
    RRSYRLSMKV KAFPSPEIVW LKDGSPATLK SARYLVHGYS LIIKDVTTED 400
    AGDYTILLGI KQSRLFKNLT ATLIVNVKPQ IYEKSVSSLP SPPLYPLGSR 450
    QVLTCTVYGI PRPTITWLWH PCHHNHSKER YDFCTENEES FILDPSSNLG 500
    NRIESISQRM TVIEGTNKTV STLVVADSQT PGIYSCRAFN KIGTVERNIK 550
    FYVTDVPNGF HVSLEKMPAE GEDLKLSCVV NKFLYRDITW ILLRTVNNRT 600
    MHHSISKQKM ATTQDYSITL NLVIKNVSLE DSGTYACRAR NIYTGEDILR 650
    KTEVLVRDSE APHLLQNLSD YEVSISGSTT LDCQARGVPA PQITWFKNNH 700
    KIQQEPGIIL GPGNSTLFIE RVTEEDEGVY RCRATNQKGA VESAAYLTVQ 750
    GTSDKSNLEL ITLTCTCVAA TLFWLLLTLF IRKLKRSSSE VKTDYLSIIM 800
    DPDEVPLDEQ CERLPYDASK WEFARERLKL GKSLGRGAFG KVVQASAFGI 850
    KKSPTCRTVA VKMLKEGATA SEYKALMTEL KILTHIGHHL NVVNLLGACT 900
    KQGGPLMVIV EYCKYGNLSN YLKSKRDLFC LNKDAALHME LKKESLEPGL 950
    EQGQKPRLDS VSSSSVTSSS FPEDRSVSDV EGDEDYSEIS KQPLTMEDLI 1000
    SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN 1050
    PDYVRRGDTR LPLKWMAPES IFDKVYSTKS DVWSYGVLLW EIFSLGGSPY 1100
    PGVQMDEDFC SRLKEGMRMR TPEYATPEIY QIMLDCWHKD PKERPRFAEL 1150
    VEKLGDLLQA NVQQDGKDYI PLNAILTRNS SFTYSTPTFS EDLFKDGFAD 1200
    PHFHSGSSDD VRYVNAFKFM SLERIKTFEE LSPNSTSMFE DYQLDTSTLL 1250
    GSPLLKRFTW TETKPKASMK IDLRIASKSK EAGLSDLPRP SFCFSSCGHI 1300
    RPVQDDESEL GKESCCSPPP DYNSVVLYSS PPA 1333
    Length:1,333
    Mass (Da):149,876
    Last modified:June 1, 1994 - v1
    Checksum:iC06533B7ECBC404C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti158 – 1581Missing in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti211 – 2111Missing in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti245 – 2451H → L in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti603 – 6031H → N in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti609 – 6157KMATTQD → NGHHSS in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti696 – 6961F → L in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti734 – 7341A → S in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti765 – 7651C → Y in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti820 – 8201K → N in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti1009 – 10091G → R in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti1181 – 11811S → G in BAA24498. (PubMed:9524283)Curated
    Sequence conflicti1181 – 11811S → N in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti1193 – 11942LF → RG in CAA55311. (PubMed:8134130)Curated
    Sequence conflicti1278 – 12792KS → PR in CAA55311. (PubMed:8134130)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07297 mRNA. Translation: AAA40078.1.
    X78568 mRNA. Translation: CAA55311.1.
    D88689 mRNA. Translation: BAA24498.1.
    CCDSiCCDS19879.1.
    PIRiI78875.
    S49010.
    RefSeqiNP_034358.2. NM_010228.3.
    UniGeneiMm.389712.

    Genome annotation databases

    EnsembliENSMUST00000031653; ENSMUSP00000031653; ENSMUSG00000029648.
    GeneIDi14254.
    KEGGimmu:14254.
    UCSCiuc009aoh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07297 mRNA. Translation: AAA40078.1 .
    X78568 mRNA. Translation: CAA55311.1 .
    D88689 mRNA. Translation: BAA24498.1 .
    CCDSi CCDS19879.1.
    PIRi I78875.
    S49010.
    RefSeqi NP_034358.2. NM_010228.3.
    UniGenei Mm.389712.

    3D structure databases

    ProteinModelPortali P35969.
    SMRi P35969. Positions 32-751, 788-1197.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199706. 5 interactions.
    DIPi DIP-39359N.
    IntActi P35969. 8 interactions.
    MINTi MINT-4139959.

    Chemistry

    BindingDBi P35969.
    ChEMBLi CHEMBL3516.

    PTM databases

    PhosphoSitei P35969.

    Proteomic databases

    PaxDbi P35969.
    PRIDEi P35969.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031653 ; ENSMUSP00000031653 ; ENSMUSG00000029648 .
    GeneIDi 14254.
    KEGGi mmu:14254.
    UCSCi uc009aoh.1. mouse.

    Organism-specific databases

    CTDi 2321.
    MGIi MGI:95558. Flt1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108679.
    HOGENOMi HOG000037949.
    HOVERGENi HBG053432.
    InParanoidi P35969.
    KOi K05096.
    OrthoDBi EOG75F4CC.
    PhylomeDBi P35969.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.
    Reactomei REACT_205099. VEGF binds to VEGFR leading to receptor dimerization.
    REACT_227870. Neurophilin interactions with VEGF and VEGFR.

    Miscellaneous databases

    ChiTaRSi FLT1. mouse.
    NextBioi 285579.
    PROi P35969.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35969.
    Bgeei P35969.
    CleanExi MM_FLT1.
    Genevestigatori P35969.

    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.
    IPR013106. Ig_V-set.
    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. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 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. 5 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

    1. "Molecular cloning of murine FLT and FLT4."
      Finnerty H., Kelleher K., Morris G.E., Bean K., Merberg D.M., Kriz R., Morris J.C., Sookdeo H., Turner K.J., Wood C.R.
      Oncogene 8:2293-2298(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Neonatal brain and Placenta.
    2. "Isolation of a gene encoding a novel receptor tyrosine kinase from differentiated embryonic stem cells."
      Choi K., Wall C., Hanratty R., Keller G.
      Oncogene 9:1261-1266(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Genomic organization of the flt-1 gene encoding for vascular endothelial growth factor (VEGF) receptor-1 suggests an intimate evolutionary relationship between the 7-Ig and the 5-Ig tyrosine kinase receptors."
      Kondo K., Hiratsuka S., Subbalakshmi E., Matsushime H., Shibuya M.
      Gene 208:297-305(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Lung.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 110-119 AND 185-191, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    5. "Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium."
      Fong G.H., Rossant J., Gertsenstein M., Breitman M.L.
      Nature 376:66-70(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN BLOOD VESSEL DEVELOPMENT DURING EMBRYOGENESIS.
    6. "Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice."
      Hiratsuka S., Minowa O., Kuno J., Noda T., Shibuya M.
      Proc. Natl. Acad. Sci. U.S.A. 95:9349-9354(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN MACROPHAGE MIGRATION.
    7. "Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis."
      Hiratsuka S., Maru Y., Okada A., Seiki M., Noda T., Shibuya M.
      Cancer Res. 61:1207-1213(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS.
    8. "The VEGF receptor flt-1 (VEGFR-1) is a positive modulator of vascular sprout formation and branching morphogenesis."
      Kearney J.B., Kappas N.C., Ellerstrom C., DiPaola F.W., Bautch V.L.
      Blood 103:4527-4535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    9. "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 ANGIOGENESIS.
    10. "Vascular endothelial growth factor receptor-1 signaling promotes mobilization of macrophage lineage cells from bone marrow and stimulates solid tumor growth."
      Muramatsu M., Yamamoto S., Osawa T., Shibuya M.
      Cancer Res. 70:8211-8221(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiVGFR1_MOUSE
    AccessioniPrimary (citable) accession number: P35969
    Secondary accession number(s): O55094, Q61517
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 155 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3