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P35917

- VGFR3_MOUSE

UniProt

P35917 - VGFR3_MOUSE

Protein

Vascular endothelial growth factor receptor 3

Gene

Flt4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (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 VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'.6 Publications

    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 VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei879 – 8791ATPPROSITE-ProRule annotation
    Active sitei1037 – 10371Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi851 – 8599ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. vascular endothelial growth factor-activated receptor activity Source: MGI

    GO - Biological processi

    1. blood vessel morphogenesis Source: UniProtKB
    2. lymphangiogenesis Source: UniProtKB
    3. lymph vessel development Source: BHF-UCL
    4. negative regulation of apoptotic process Source: Ensembl
    5. positive regulation of cell proliferation Source: MGI
    6. positive regulation of endothelial cell migration Source: Ensembl
    7. positive regulation of endothelial cell proliferation Source: Ensembl
    8. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
    9. positive regulation of JNK cascade Source: Ensembl
    10. positive regulation of protein kinase C signaling Source: Ensembl
    11. positive regulation of protein phosphorylation Source: Ensembl
    12. positive regulation vascular endothelial growth factor production Source: Ensembl
    13. protein autophosphorylation Source: Ensembl
    14. regulation of blood vessel remodeling Source: UniProtKB
    15. sprouting angiogenesis Source: UniProtKB
    16. vascular endothelial growth factor receptor signaling pathway Source: InterPro
    17. vascular endothelial growth factor signaling pathway Source: GOC
    18. vasculature development Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis

    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vascular endothelial growth factor receptor 3 (EC:2.7.10.1)
    Short name:
    VEGFR-3
    Alternative name(s):
    Fms-like tyrosine kinase 4
    Short name:
    FLT-4
    Tyrosine-protein kinase receptor FLT4
    Gene namesi
    Name:Flt4
    Synonyms:Flt-4, Vegfr3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95561. Flt4.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cytoplasm 1 Publication. Nucleus By similarity
    Note: Ligand-mediated autophosphorylation leads to rapid internalization.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: InterPro
    3. nucleus Source: UniProtKB-SubCell
    4. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic lethality at about 13 dpc, due to failure of remodeling of the yolk sac capillary network and defects in remodeling and maturation of primary vascular networks.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 13631339Vascular endothelial growth factor receptor 3PRO_0000016777Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi51 ↔ 111PROSITE-ProRule annotation
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi158 ↔ 206PROSITE-ProRule annotation
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi252 ↔ 310PROSITE-ProRule annotation
    Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi411 – 4111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi445 ↔ 534PROSITE-ProRule annotation
    Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi527 – 5271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi578 ↔ 653PROSITE-ProRule annotation
    Glycosylationi582 – 5821N-linked (GlcNAc...)1 Publication
    Glycosylationi594 – 5941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi683 – 6831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi699 ↔ 751PROSITE-ProRule annotation
    Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
    Modified residuei830 – 8301Phosphotyrosine; by SRCBy similarity
    Modified residuei833 – 8331Phosphotyrosine; by SRCBy similarity
    Modified residuei1063 – 10631Phosphotyrosine; by autocatalysis and SRCBy similarity
    Modified residuei1068 – 10681Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1230 – 12301Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1231 – 12311Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1265 – 12651Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1333 – 13331Phosphotyrosine; by autocatalysis and SRCBy similarity
    Modified residuei1337 – 13371Phosphotyrosine; by autocatalysis and SRCBy similarity
    Modified residuei1363 – 13631Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    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 in response to H2O2 is mediated by a process that requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is required for autophosphorylation at additional tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction with CRK and subsequent activation of MAPK8. Phosphorylation at Tyr-1230, Tyr-1231 and Tyr-1337 is important for interaction with GRB2 and subsequent activation of the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1 signaling pathways. In response to endothelial cell adhesion onto collagen, can also be phosphorylated in the absence of FLT4 kinase activity by SRC By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP35917.
    PRIDEiP35917.

    PTM databases

    PhosphoSiteiP35917.

    Expressioni

    Tissue specificityi

    Expressed in adult lung and liver, and in fetal liver, brain, intestine and placenta.1 Publication

    Gene expression databases

    ArrayExpressiP35917.
    BgeeiP35917.
    CleanExiMM_FLT4.
    GenevestigatoriP35917.

    Interactioni

    Subunit structurei

    Interacts with VEGFC and VEGFD. Monomer in the absence of bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or VEGFD. Can also form a heterodimer with KDR. Interacts with PTPN14; the interaction is enhanced by stimulation with VEGFC. Interacts with CRK, GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-2. Identified in a complex with SRC and ITGB1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KdrP359182EBI-7845747,EBI-1555005

    Protein-protein interaction databases

    BioGridi199709. 3 interactions.
    DIPiDIP-60714N.
    IntActiP35917. 1 interaction.
    MINTiMINT-5313593.
    STRINGi10090.ENSMUSP00000020617.

    Structurei

    3D structure databases

    ProteinModelPortaliP35917.
    SMRiP35917. Positions 27-765, 821-1223.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 775751ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini797 – 1363567CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei776 – 79621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 11875Ig-like C2-type 1Add
    BLAST
    Domaini151 – 21363Ig-like C2-type 2Add
    BLAST
    Domaini230 – 32697Ig-like C2-type 3Add
    BLAST
    Domaini331 – 41585Ig-like C2-type 4Add
    BLAST
    Domaini422 – 552131Ig-like C2-type 5Add
    BLAST
    Domaini555 – 671117Ig-like C2-type 6Add
    BLAST
    Domaini678 – 76487Ig-like C2-type 7Add
    BLAST
    Domaini845 – 1173329Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The first and second Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC 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.
    HOGENOMiHOG000037949.
    HOVERGENiHBG053432.
    InParanoidiP35917.
    KOiK05097.
    OMAiPAHADIK.
    OrthoDBiEOG75F4CC.
    PhylomeDBiP35917.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 9 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.
    IPR009137. VEGFR3_rcpt.
    [Graphical view]
    PANTHERiPTHR24416:SF49. PTHR24416:SF49. 1 hit.
    PfamiPF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR01835. VEGFRECEPTR3.
    SMARTiSM00409. IG. 4 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.

    P35917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQPGAALNLR LWLCLGLLQG LANGYSMTPP TLNITEDSYV IDTGDSLSIS     50
    CRGQHPLEWT WPGAQEVLTT GGKDSEDTRV VHDCEGTEAR PYCKVLLLAQ 100
    THANNTGSYH CYYKYIKARI EGTTAASTYV FVRDFKHPFI NKPDTLLVNR 150
    KDSMWVPCLV SIPGLNITLR SQSSALHPDG QEVLWDDRRG MRVPTQLLRD 200
    ALYLQCETTW GDQNFLSNLF VVHITGNELY DIQLYPKKSM ELLVGEKLVL 250
    NCTVWAEFDS GVTFDWDYPG KQAERAKWVP ERRSQQTHTE LSSILTIHNV 300
    SQNDLGPYVC EANNGIQRFR ESTEVIVHEK PFISVEWLKG PVLEATAGDE 350
    LVKLPVKLAA YPPPEFQWYK DRKAVTGRHN PHALVLKEVT EASAGVYTLA 400
    LWNSAAGLRQ NISLELVVNV PPHIHEKEAS SPSIYSRHSR QTLTCTAYGV 450
    PQPLSVQWHW RPWTPCKTFA QRSLRRRQQR DGMPQCRDWK EVTTQDAVNP 500
    IESLDSWTEF VEGKNKTVSK LVIQDANVSA MYKCVVVNKV GQDERLIYFY 550
    VTTIPDGFSI ESEPSEDPLE GQSVRLSCRA DNYTYEHLRW YRLNLSTLHD 600
    AQGNPLLLDC KNVHLFATPL EANLEEAEPG ARHATLSLNI PRVAPEDEGD 650
    YVCEVQDRRS QDKHCHKKYL SVQALEAPRL TQNLTDLLVN VSDSLEMRCP 700
    VAGAHVPSIV WYKDERLLEK ESGIDLADSN QRLSIQRVRE EDAGRYLCSV 750
    CNAKGCVNSS ASVAVEGSED KGSMEIVILI GTGVIAVFFW VLLLLIFCNM 800
    KRPAHADIKT GYLSIIMDPG EVPLEEQCEY LSYDASQWEF PRERLHLGRV 850
    LGHGAFGKVV EASAFGINKG SSCDTVAVKM LKEGATASEH RALMSELKIL 900
    IHIGNHLNVV NLLGACTKPN GPLMVIVEFC KYGNLSNFLR VKRDTFNPYA 950
    EKSPEQRRRF RAMVEGAKAD RRRPGSSDRA LFTRFLMGKG SARRAPLVQE 1000
    AEDLWLSPLT MEDLVCYSFQ VARGMEFLAS RKCIHRDLAA RNILLSESDI 1050
    VKICDFGLAR DIYKDPDYVR KGSARLPLKW MAPESIFDKV YTTQSDVWSF 1100
    GVLLWEIFSL GASPYPGVQI NEEFCQRLKD GTRMRAPELA TPAIRHIMQS 1150
    CWSGDPKARP AFSDLVEILG DLLQGGGWQE EEEERMALHS SQSSEEDGFM 1200
    QASTTALHIT EADADDSPPS MHCHSLAARY YNCVSFPGRL ARGTKTPGSS 1250
    RMKTFEELPM TPTTYKASMD NQTDSGMVLA SEEFEELESR HRPEGSFSCK 1300
    GPGQHMDIPR GHPDPQGRRR RPTQGAQGGK VFYNNEYGEV SQPCTEGDCC 1350
    PSAGSTFFAD SSY 1363
    Length:1,363
    Mass (Da):153,016
    Last modified:June 1, 1994 - v1
    Checksum:iF1BF8A2BDEF99BE9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07296 mRNA. Translation: AAA40077.1.
    CCDSiCCDS24618.1.
    PIRiI58375.
    RefSeqiNP_032055.1. NM_008029.3.
    UniGeneiMm.3291.

    Genome annotation databases

    EnsembliENSMUST00000020617; ENSMUSP00000020617; ENSMUSG00000020357.
    GeneIDi14257.
    KEGGimmu:14257.
    UCSCiuc007iqu.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07296 mRNA. Translation: AAA40077.1 .
    CCDSi CCDS24618.1.
    PIRi I58375.
    RefSeqi NP_032055.1. NM_008029.3.
    UniGenei Mm.3291.

    3D structure databases

    ProteinModelPortali P35917.
    SMRi P35917. Positions 27-765, 821-1223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199709. 3 interactions.
    DIPi DIP-60714N.
    IntActi P35917. 1 interaction.
    MINTi MINT-5313593.
    STRINGi 10090.ENSMUSP00000020617.

    Chemistry

    BindingDBi P35917.

    PTM databases

    PhosphoSitei P35917.

    Proteomic databases

    PaxDbi P35917.
    PRIDEi P35917.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020617 ; ENSMUSP00000020617 ; ENSMUSG00000020357 .
    GeneIDi 14257.
    KEGGi mmu:14257.
    UCSCi uc007iqu.2. mouse.

    Organism-specific databases

    CTDi 2324.
    MGIi MGI:95561. Flt4.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000037949.
    HOVERGENi HBG053432.
    InParanoidi P35917.
    KOi K05097.
    OMAi PAHADIK.
    OrthoDBi EOG75F4CC.
    PhylomeDBi P35917.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.
    Reactomei REACT_205099. VEGF binds to VEGFR leading to receptor dimerization.

    Miscellaneous databases

    NextBioi 285591.
    PROi P35917.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35917.
    Bgeei P35917.
    CleanExi MM_FLT4.
    Genevestigatori P35917.

    Family and domain databases

    Gene3Di 2.60.40.10. 9 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.
    IPR009137. VEGFR3_rcpt.
    [Graphical view ]
    PANTHERi PTHR24416:SF49. PTHR24416:SF49. 1 hit.
    Pfami PF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR01835. VEGFRECEPTR3.
    SMARTi SM00409. IG. 4 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: C57BL/6J.
    2. "Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene."
      Galland F., Karamysheva A., Mattei M.-G., Rosnet O., Marchetto S., Birnbaum D.
      Genomics 13:475-478(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1033-1072.
    3. "Cardiovascular failure in mouse embryos deficient in VEGF receptor-3."
      Dumont D.J., Jussila L., Taipale J., Lymboussaki A., Mustonen T., Pajusola K., Breitman M., Alitalo K.
      Science 282:946-949(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    4. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-582.
      Strain: C57BL/6.
      Tissue: Plasma.
    5. Cited for: FUNCTION, TISSUE SPECIFICITY.
    6. "VEGFR-3 ligand-binding and kinase activity are required for lymphangiogenesis but not for angiogenesis."
      Zhang L., Zhou F., Han W., Shen B., Luo J., Shibuya M., He Y.
      Cell Res. 20:1319-1331(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LYMPHANGIOGENESIS.
    7. Cited for: FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS, SUBCELLULAR LOCATION.
    8. "Soluble vascular endothelial growth factor receptor-3 suppresses lymphangiogenesis and lymphatic metastasis in bladder cancer."
      Yang H., Kim C., Kim M.J., Schwendener R.A., Alitalo K., Heston W., Kim I., Kim W.J., Koh G.Y.
      Mol. Cancer 10:36-36(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LYMPHANGIOGENESIS, ROLE IN CANCER.
    9. Cited for: FUNCTION.

    Entry informationi

    Entry nameiVGFR3_MOUSE
    AccessioniPrimary (citable) accession number: P35917
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 149 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, 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