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P35968

- VGFR2_HUMAN

UniProt

P35968 - VGFR2_HUMAN

Protein

Vascular endothelial growth factor receptor 2

Gene

KDR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC.22 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.2 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by the small molecule PTK inhibitor SU5614 ((3Z)-5-Chloro-3-[(3,5-dimethyl-1H-pyrrol-2-yl)methylene]-1,3-dihydro-2H-indol-2-one). May be regulated by hydrogen sulfide (H2S) levels via a H2S-sensitive intracellular disulfide bond.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei868 – 8681ATPCurated
    Active sitei1028 – 10281Proton acceptorPROSITE-ProRule annotation
    Sitei1175 – 11751Interaction with SHBBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi840 – 8489ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. growth factor binding Source: BHF-UCL
    3. Hsp90 protein binding Source: BHF-UCL
    4. integrin binding Source: BHF-UCL
    5. protein binding Source: BHF-UCL
    6. protein tyrosine kinase activity Source: UniProtKB
    7. receptor signaling protein tyrosine kinase activity Source: BHF-UCL
    8. transmembrane receptor protein tyrosine kinase activity Source: BHF-UCL
    9. vascular endothelial growth factor-activated receptor activity Source: UniProtKB
    10. vascular endothelial growth factor binding Source: BHF-UCL

    GO - Biological processi

    1. angiogenesis Source: BHF-UCL
    2. branching morphogenesis of an epithelial tube Source: Ensembl
    3. calcium ion homeostasis Source: Ensembl
    4. calcium-mediated signaling using intracellular calcium source Source: UniProtKB
    5. cell fate commitment Source: Ensembl
    6. cell maturation Source: Ensembl
    7. cell migration involved in sprouting angiogenesis Source: BHF-UCL
    8. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
    9. embryonic hemopoiesis Source: UniProtKB
    10. endothelial cell differentiation Source: Ensembl
    11. endothelium development Source: UniProtKB
    12. extracellular matrix organization Source: Reactome
    13. lung alveolus development Source: Ensembl
    14. lymph vessel development Source: Ensembl
    15. negative regulation of apoptotic process Source: UniProtKB
    16. negative regulation of endothelial cell apoptotic process Source: UniProtKB
    17. ovarian follicle development Source: Ensembl
    18. peptidyl-tyrosine autophosphorylation Source: BHF-UCL
    19. peptidyl-tyrosine phosphorylation Source: UniProtKB
    20. positive regulation of angiogenesis Source: UniProtKB
    21. positive regulation of cell migration Source: UniProtKB
    22. positive regulation of cell proliferation Source: UniProtKB
    23. positive regulation of endothelial cell migration Source: BHF-UCL
    24. positive regulation of endothelial cell proliferation Source: UniProtKB
    25. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    26. positive regulation of focal adhesion assembly Source: BHF-UCL
    27. positive regulation of MAPK cascade Source: UniProtKB
    28. positive regulation of mesenchymal cell proliferation Source: Ensembl
    29. positive regulation of nitric-oxide synthase biosynthetic process Source: UniProtKB
    30. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    31. positive regulation of positive chemotaxis Source: BHF-UCL
    32. positive regulation of protein phosphorylation Source: UniProtKB
    33. positive regulation of vasculogenesis Source: UniProtKB
    34. protein autophosphorylation Source: UniProtKB
    35. regulation of cell shape Source: BHF-UCL
    36. signal transduction by phosphorylation Source: GOC
    37. surfactant homeostasis Source: Ensembl
    38. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
    39. vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    40. vascular endothelial growth factor signaling pathway Source: GOC
    41. vasculogenesis Source: UniProtKB
    42. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Angiogenesis, Differentiation, Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_12473. Neurophilin interactions with VEGF and VEGFR.
    REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
    REACT_13552. Integrin cell surface interactions.
    SignaLinkiP35968.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vascular endothelial growth factor receptor 2 (EC:2.7.10.1)
    Short name:
    VEGFR-2
    Alternative name(s):
    Fetal liver kinase 1
    Short name:
    FLK-1
    Kinase insert domain receptor
    Short name:
    KDR
    Protein-tyrosine kinase receptor flk-1
    CD_antigen: CD309
    Gene namesi
    Name:KDR
    Synonyms:FLK1, VEGFR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6307. KDR.

    Subcellular locationi

    Isoform 1 : Cell membrane; Single-pass type I membrane protein. Cytoplasm. Nucleus. Cytoplasmic vesicle. Early endosome
    Note: Detected on caveolae-enriched lipid rafts at the cell surface. Is recycled from the plasma membrane to endosomes and back again. Phosphorylation triggered by VEGFA binding promotes internalization and subsequent degradation. VEGFA binding triggers internalization and translocation to the nucleus.
    Cell junction By similarity
    Note: Localized with RAP1A at cell-cell junctions.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. early endosome Source: BHF-UCL
    4. endosome Source: UniProtKB
    5. external side of plasma membrane Source: Ensembl
    6. extracellular region Source: UniProtKB-SubCell
    7. Golgi apparatus Source: UniProtKB
    8. integral component of plasma membrane Source: UniProtKB
    9. membrane raft Source: UniProtKB
    10. nucleus Source: UniProtKB-SubCell
    11. plasma membrane Source: UniProtKB
    12. sorting endosome Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane, Nucleus, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Hemangioma, capillary infantile (HCI) [MIM:602089]: A condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring.2 Publications
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti482 – 4821C → R in HCI susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced and KDR activity is increased compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation predicts to result in loss-of-function and disruption of the normal association of these molecules. 2 Publications
    Corresponds to variant rs34231037 [ dbSNP | Ensembl ].
    VAR_042057
    Natural varianti1147 – 11471P → S in HCI; somatic mutation. 1 Publication
    VAR_063147
    Plays a major role in tumor angiogenesis. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi726 – 7261R → A: Strongly reduced autophosphorylation and activation of MAP kinases. 1 Publication
    Mutagenesisi731 – 7311D → A: Strongly reduced autophosphorylation and activation of MAP kinases. 1 Publication
    Mutagenesisi801 – 8011Y → F: Abolishes stimulation of nitric oxide synthesis. 1 Publication
    Mutagenesisi868 – 8681K → M: Loss of enzyme activity. 1 Publication
    Mutagenesisi951 – 9511Y → F: Abolishes reorganization of the actin cytoskeleton and cell migration in response to VEGFA. 1 Publication
    Mutagenesisi996 – 9961Y → F: Strongly reduced autophosphorylation. Reduces phosphorylation of PLCG1. 1 Publication
    Mutagenesisi1045 – 10451C → A: Significantly higher kinase activity. 1 Publication
    Mutagenesisi1054 – 10541Y → F: Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1059. 1 Publication
    Mutagenesisi1059 – 10591Y → F: Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1054. 1 Publication
    Mutagenesisi1175 – 11751Y → F: Abolishes phosphorylation of PLCG1 and MAP kinases in response to VEGFA. 1 Publication
    Mutagenesisi1214 – 12141Y → F: Loss of phosphorylation site. Abolishes reorganization of the actin cytoskeleton in response to VEGFA. 1 Publication

    Organism-specific databases

    MIMi602089. phenotype.
    Orphaneti91415. Familial capillary hemangioma.
    PharmGKBiPA30086.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 13561337Vascular endothelial growth factor receptor 2PRO_0000016771Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi53 ↔ 103PROSITE-ProRule annotation
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi143 – 1431N-linked (GlcNAc...)2 Publications
    Disulfide bondi150 ↔ 200
    Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi245 – 2451N-linked (GlcNAc...)3 Publications
    Disulfide bondi246 ↔ 307
    Glycosylationi318 – 3181N-linked (GlcNAc...)3 Publications
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi445 ↔ 530PROSITE-ProRule annotation
    Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi523 – 5231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi571 ↔ 642PROSITE-ProRule annotation
    Glycosylationi580 – 5801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi613 – 6131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi675 – 6751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi688 ↔ 737PROSITE-ProRule annotation
    Glycosylationi704 – 7041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
    Modified residuei801 – 8011Phosphotyrosine3 Publications
    Modified residuei951 – 9511Phosphotyrosine; by autocatalysis4 Publications
    Modified residuei982 – 9821Phosphoserine2 Publications
    Modified residuei984 – 9841Phosphoserine2 Publications
    Modified residuei996 – 9961Phosphotyrosine; by autocatalysis3 Publications
    Disulfide bondi1024 ↔ 1045Redox-active
    Modified residuei1054 – 10541Phosphotyrosine; by autocatalysis6 Publications
    Modified residuei1059 – 10591Phosphotyrosine; by autocatalysis7 Publications
    Modified residuei1175 – 11751Phosphotyrosine; by autocatalysis4 Publications
    Modified residuei1214 – 12141Phosphotyrosine; by autocatalysis5 Publications
    Modified residuei1305 – 13051Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei1309 – 13091Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei1319 – 13191Phosphotyrosine; by autocatalysis2 Publications

    Post-translational modificationi

    N-glycosylated.3 Publications
    Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases.3 Publications
    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-951 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1175 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1214 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRB. Dephosphorylated by PTPRJ at Tyr-951, Tyr-996, Tyr-1054, Tyr-1059, Tyr-1175 and Tyr-1214.8 Publications
    The inhibitory disulfide bond between Cys-1024 and Cys-1045 may serve as a specific molecular switch for H2S-induced modification that regulates VEGFR2 function.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP35968.
    PRIDEiP35968.

    PTM databases

    PhosphoSiteiP35968.

    Expressioni

    Tissue specificityi

    Detected in cornea (at protein level). Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiP35968.
    BgeeiP35968.
    CleanExiHS_KDR.
    GenevestigatoriP35968.

    Organism-specific databases

    HPAiCAB004028.

    Interactioni

    Subunit structurei

    Homodimer in the presence of bound dimeric VEGFA, VEGFC or VEGFD ligands; monomeric in the absence of bound ligands. Can also form heterodimers with FLT1/VEGFR1 and FLT4/VEGFR2. Interacts (tyrosine phosphorylated) with LFYN, NCK1, PLCG1. Interacts (tyrosine-phosphorylated active form preferentially) with DAB2IP (via C2 domain and active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts with SHBSH2D2A/TSAD, GRB2, MYOF, CBL and PDCD6. Interacts with HIV-1 Tat.22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRKP461082EBI-1005487,EBI-886
    FLT4P359165EBI-1005487,EBI-1005467
    GREM1O605654EBI-1005487,EBI-944395
    HSPG2P981604EBI-1005487,EBI-947664
    METP085813EBI-1005487,EBI-1039152
    NCK1P163333EBI-1005487,EBI-389883
    NRP1O147862EBI-1005487,EBI-1187100
    PDCD6O753404EBI-1005487,EBI-352915
    PTPRJQ129134EBI-1005487,EBI-2264500
    SRCP129312EBI-1005487,EBI-621482
    VEGFAP156924EBI-1005487,EBI-1026643
    VEGFAP15692-45EBI-1005487,EBI-1026691

    Protein-protein interaction databases

    BioGridi109992. 29 interactions.
    DIPiDIP-486N.
    IntActiP35968. 21 interactions.
    MINTiMINT-127732.
    STRINGi9606.ENSP00000263923.

    Structurei

    Secondary structure

    1
    1356
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi134 – 1385
    Beta strandi145 – 1484
    Beta strandi152 – 1543
    Beta strandi159 – 1646
    Turni165 – 1673
    Beta strandi168 – 1703
    Beta strandi174 – 1763
    Beta strandi178 – 1803
    Turni181 – 1833
    Beta strandi184 – 1885
    Helixi189 – 1913
    Turni192 – 1943
    Beta strandi196 – 2027
    Beta strandi214 – 2185
    Beta strandi223 – 2308
    Beta strandi234 – 2385
    Beta strandi242 – 2509
    Beta strandi257 – 2615
    Helixi269 – 2724
    Beta strandi279 – 2824
    Beta strandi285 – 29612
    Helixi299 – 3013
    Beta strandi303 – 3108
    Beta strandi315 – 32814
    Beta strandi676 – 6794
    Beta strandi684 – 6874
    Beta strandi697 – 70610
    Beta strandi713 – 7164
    Turni717 – 7204
    Beta strandi721 – 7244
    Helixi729 – 7313
    Beta strandi733 – 7408
    Beta strandi746 – 75510
    Helixi760 – 79435
    Beta strandi804 – 8063
    Turni808 – 8103
    Turni813 – 8153
    Helixi817 – 8193
    Helixi824 – 8274
    Helixi831 – 8333
    Beta strandi834 – 8429
    Beta strandi844 – 85815
    Beta strandi862 – 8709
    Helixi876 – 89217
    Beta strandi901 – 9055
    Beta strandi907 – 9104
    Beta strandi913 – 9175
    Helixi924 – 9296
    Turni930 – 9334
    Beta strandi934 – 9363
    Turni995 – 9984
    Helixi1002 – 102120
    Beta strandi1024 – 10263
    Helixi1031 – 10333
    Beta strandi1034 – 10363
    Helixi1038 – 10403
    Beta strandi1042 – 10443
    Helixi1048 – 10503
    Turni1053 – 10553
    Beta strandi1059 – 10624
    Beta strandi1065 – 10673
    Helixi1069 – 10713
    Helixi1074 – 10796
    Helixi1084 – 109916
    Beta strandi1105 – 11084
    Helixi1113 – 11219
    Helixi1133 – 114210
    Helixi1147 – 11493
    Helixi1153 – 116715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VR2X-ray2.40A806-1171[»]
    1Y6AX-ray2.10A806-1171[»]
    1Y6BX-ray2.10A806-1171[»]
    1YWNX-ray1.71A806-1171[»]
    2M59NMR-A/B759-795[»]
    2OH4X-ray2.05A806-1171[»]
    2P2HX-ray1.95A815-1171[»]
    2P2IX-ray2.40A/B815-1171[»]
    2QU5X-ray2.95A815-1171[»]
    2QU6X-ray2.10A/B815-1171[»]
    2RL5X-ray2.65A815-1171[»]
    2X1WX-ray2.70L/M/N/O120-326[»]
    2X1XX-ray3.10R120-326[»]
    2XIRX-ray1.50A806-1171[»]
    3B8QX-ray2.75A/B815-1171[»]
    3B8RX-ray2.70A/B815-1171[»]
    3BE2X-ray1.75A815-1171[»]
    3C7QX-ray2.10A806-1171[»]
    3CJFX-ray2.15A806-1168[»]
    3CJGX-ray2.25A806-1168[»]
    3CP9X-ray2.50A/B815-1171[»]
    3CPBX-ray2.70A/B815-1171[»]
    3CPCX-ray2.40A/B815-1171[»]
    3DTWX-ray2.90A/B815-1171[»]
    3EFLX-ray2.20A/B815-1171[»]
    3EWHX-ray1.60A815-1171[»]
    3KVQX-ray2.70A657-764[»]
    3S35X-ray2.20X220-338[»]
    3S36X-ray3.20X220-338[»]
    3S37X-ray2.70X220-338[»]
    3U6JX-ray2.15A815-1171[»]
    3V2AX-ray3.20R2-764[»]
    3V6BX-ray3.20R132-548[»]
    3VHEX-ray1.55A811-1169[»]
    3VHKX-ray2.49A806-1171[»]
    3VIDX-ray2.30A813-1168[»]
    3VNTX-ray1.64A806-1171[»]
    3VO3X-ray1.52A806-1171[»]
    4AG8X-ray1.95A806-1171[»]
    4AGCX-ray2.00A787-1171[»]
    4AGDX-ray2.81A787-1171[»]
    4ASDX-ray2.03A787-1171[»]
    4ASEX-ray1.83A787-1171[»]
    ProteinModelPortaliP35968.
    SMRiP35968. Positions 32-756, 759-795, 815-1209.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35968.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 764745ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini786 – 1356571CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei765 – 78521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 11065Ig-like C2-type 1Add
    BLAST
    Domaini141 – 20767Ig-like C2-type 2Add
    BLAST
    Domaini224 – 32097Ig-like C2-type 3Add
    BLAST
    Domaini328 – 41487Ig-like C2-type 4Add
    BLAST
    Domaini421 – 548128Ig-like C2-type 5Add
    BLAST
    Domaini551 – 660110Ig-like C2-type 6Add
    BLAST
    Domaini667 – 75387Ig-like C2-type 7Add
    BLAST
    Domaini834 – 1162329Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding.1 Publication

    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.
    HOVERGENiHBG053432.
    InParanoidiP35968.
    KOiK05098.
    OMAiISYAGMV.
    OrthoDBiEOG75F4CC.
    PhylomeDBiP35968.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 8 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.
    IPR009136. VEGFR2_rcpt.
    [Graphical view]
    PANTHERiPTHR24416:SF45. PTHR24416:SF45. 1 hit.
    PfamiPF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    PRINTSiPR01834. VEGFRECEPTR2.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35968-1) [UniParc]FASTAAdd to Basket

    Also known as: mbVegfr-2

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

    « Hide

    MQSKVLLAVA LWLCVETRAA SVGLPSVSLD LPRLSIQKDI LTIKANTTLQ     50
    ITCRGQRDLD WLWPNNQSGS EQRVEVTECS DGLFCKTLTI PKVIGNDTGA 100
    YKCFYRETDL ASVIYVYVQD YRSPFIASVS DQHGVVYITE NKNKTVVIPC 150
    LGSISNLNVS LCARYPEKRF VPDGNRISWD SKKGFTIPSY MISYAGMVFC 200
    EAKINDESYQ SIMYIVVVVG YRIYDVVLSP SHGIELSVGE KLVLNCTART 250
    ELNVGIDFNW EYPSSKHQHK KLVNRDLKTQ SGSEMKKFLS TLTIDGVTRS 300
    DQGLYTCAAS SGLMTKKNST FVRVHEKPFV AFGSGMESLV EATVGERVRI 350
    PAKYLGYPPP EIKWYKNGIP LESNHTIKAG HVLTIMEVSE RDTGNYTVIL 400
    TNPISKEKQS HVVSLVVYVP PQIGEKSLIS PVDSYQYGTT QTLTCTVYAI 450
    PPPHHIHWYW QLEEECANEP SQAVSVTNPY PCEEWRSVED FQGGNKIEVN 500
    KNQFALIEGK NKTVSTLVIQ AANVSALYKC EAVNKVGRGE RVISFHVTRG 550
    PEITLQPDMQ PTEQESVSLW CTADRSTFEN LTWYKLGPQP LPIHVGELPT 600
    PVCKNLDTLW KLNATMFSNS TNDILIMELK NASLQDQGDY VCLAQDRKTK 650
    KRHCVVRQLT VLERVAPTIT GNLENQTTSI GESIEVSCTA SGNPPPQIMW 700
    FKDNETLVED SGIVLKDGNR NLTIRRVRKE DEGLYTCQAC SVLGCAKVEA 750
    FFIIEGAQEK TNLEIIILVG TAVIAMFFWL LLVIILRTVK RANGGELKTG 800
    YLSIVMDPDE LPLDEHCERL PYDASKWEFP RDRLKLGKPL GRGAFGQVIE 850
    ADAFGIDKTA TCRTVAVKML KEGATHSEHR ALMSELKILI HIGHHLNVVN 900
    LLGACTKPGG PLMVIVEFCK FGNLSTYLRS KRNEFVPYKT KGARFRQGKD 950
    YVGAIPVDLK RRLDSITSSQ SSASSGFVEE KSLSDVEEEE APEDLYKDFL 1000
    TLEHLICYSF QVAKGMEFLA SRKCIHRDLA ARNILLSEKN VVKICDFGLA 1050
    RDIYKDPDYV RKGDARLPLK WMAPETIFDR VYTIQSDVWS FGVLLWEIFS 1100
    LGASPYPGVK IDEEFCRRLK EGTRMRAPDY TTPEMYQTML DCWHGEPSQR 1150
    PTFSELVEHL GNLLQANAQQ DGKDYIVLPI SETLSMEEDS GLSLPTSPVS 1200
    CMEEEEVCDP KFHYDNTAGI SQYLQNSKRK SRPVSVKTFE DIPLEEPEVK 1250
    VIPDDNQTDS GMVLASEELK TLEDRTKLSP SFGGMVPSKS RESVASEGSN 1300
    QTSGYQSGYH SDDTDTTVYS SEEAELLKLI EIGVQTGSTA QILQPDSGTT 1350
    LSSPPV 1356
    Length:1,356
    Mass (Da):151,527
    Last modified:December 1, 2000 - v2
    Checksum:i59E7C44B05CFEBB3
    GO
    Isoform 2 (identifier: P35968-2) [UniParc]FASTAAdd to Basket

    Also known as: sVegfr-2

    The sequence of this isoform differs from the canonical sequence as follows:
         663-678: ERVAPTITGNLENQTT → GRETILDHCAEAVGMP
         679-1356: Missing.

    Show »
    Length:678
    Mass (Da):75,896
    Checksum:iBD4BD2686CE95EB9
    GO
    Isoform 3 (identifier: P35968-3) [UniParc]FASTAAdd to Basket

    Also known as: VEGFR2-712

    The sequence of this isoform differs from the canonical sequence as follows:
         712-712: G → E
         713-1356: Missing.

    Show »
    Length:712
    Mass (Da):79,634
    Checksum:i1043A452AE64A528
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21Q → E in AAC16450. 1 PublicationCurated
    Sequence conflicti772 – 7721A → T in AAA59459. (PubMed:1656371)Curated
    Sequence conflicti772 – 7721A → T in CAA43837. (PubMed:1656371)Curated
    Sequence conflicti787 – 7871R → G in AAA59459. (PubMed:1656371)Curated
    Sequence conflicti787 – 7871R → G in CAA43837. (PubMed:1656371)Curated
    Sequence conflicti835 – 8351K → N in AAA59459. (PubMed:1656371)Curated
    Sequence conflicti835 – 8351K → N in CAA43837. (PubMed:1656371)Curated
    Sequence conflicti1347 – 13471S → T in AAA59459. (PubMed:1656371)Curated
    Sequence conflicti1347 – 13471S → T in CAA43837. (PubMed:1656371)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2 – 21Q → R in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042053
    Natural varianti136 – 1361V → M.1 Publication
    Corresponds to variant rs35636987 [ dbSNP | Ensembl ].
    VAR_042054
    Natural varianti248 – 2481A → G in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042055
    Natural varianti275 – 2751R → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036126
    Natural varianti297 – 2971V → I.1 Publication
    Corresponds to variant rs2305948 [ dbSNP | Ensembl ].
    VAR_022071
    Natural varianti462 – 4621L → V.1 Publication
    Corresponds to variant rs56286620 [ dbSNP | Ensembl ].
    VAR_042056
    Natural varianti472 – 4721Q → H.2 Publications
    Corresponds to variant rs1870377 [ dbSNP | Ensembl ].
    VAR_020353
    Natural varianti482 – 4821C → R in HCI susceptibility; expression of FLT1 in hemangioma endothelial cells is markedly reduced and KDR activity is increased compared to controls; low FLT1 expression in hemangioma cells is caused by reduced activity of a pathway involving ITGB1, ANTXR1, KDR and NFATC2IP; the mutation predicts to result in loss-of-function and disruption of the normal association of these molecules. 2 Publications
    Corresponds to variant rs34231037 [ dbSNP | Ensembl ].
    VAR_042057
    Natural varianti539 – 5391G → R.1 Publication
    Corresponds to variant rs55716939 [ dbSNP | Ensembl ].
    VAR_042058
    Natural varianti689 – 6891T → M.1 Publication
    Corresponds to variant rs34038364 [ dbSNP | Ensembl ].
    VAR_042059
    Natural varianti814 – 8141D → N.1 Publication
    Corresponds to variant rs35603373 [ dbSNP | Ensembl ].
    VAR_042060
    Natural varianti848 – 8481V → E Strongly reduced autophosphorylation and kinase activity. 1 Publication
    Corresponds to variant rs1139776 [ dbSNP | Ensembl ].
    VAR_046679
    Natural varianti873 – 8731G → R in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036127
    Natural varianti952 – 9521V → I.
    Corresponds to variant rs13129474 [ dbSNP | Ensembl ].
    VAR_046680
    Natural varianti1065 – 10651A → T.1 Publication
    Corresponds to variant rs56302315 [ dbSNP | Ensembl ].
    VAR_042061
    Natural varianti1147 – 11471P → S in HCI; somatic mutation. 1 Publication
    VAR_063147

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei663 – 67816ERVAP…ENQTT → GRETILDHCAEAVGMP in isoform 2. 1 PublicationVSP_041988Add
    BLAST
    Alternative sequencei679 – 1356678Missing in isoform 2. 1 PublicationVSP_041989Add
    BLAST
    Alternative sequencei712 – 7121G → E in isoform 3. 1 PublicationVSP_041990
    Alternative sequencei713 – 1356644Missing in isoform 3. 1 PublicationVSP_041991Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU826563 mRNA. Translation: ACF47599.1.
    FJ899739 mRNA. Translation: ACR78514.1.
    AF035121 mRNA. Translation: AAB88005.1.
    AF063658 mRNA. Translation: AAC16450.1.
    AC021220 Genomic DNA. No translation available.
    AC111194 Genomic DNA. No translation available.
    BC131822 mRNA. Translation: AAI31823.1.
    L04947 mRNA. Translation: AAA59459.1.
    X61656 mRNA. Translation: CAA43837.1.
    X89776 Genomic DNA. Translation: CAA61916.1.
    CCDSiCCDS3497.1. [P35968-1]
    PIRiJC1402.
    RefSeqiNP_002244.1. NM_002253.2. [P35968-1]
    UniGeneiHs.479756.

    Genome annotation databases

    EnsembliENST00000263923; ENSP00000263923; ENSG00000128052. [P35968-1]
    GeneIDi3791.
    KEGGihsa:3791.
    UCSCiuc003has.3. human. [P35968-1]
    uc011bzx.2. human. [P35968-2]

    Polymorphism databases

    DMDMi9087218.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU826563 mRNA. Translation: ACF47599.1 .
    FJ899739 mRNA. Translation: ACR78514.1 .
    AF035121 mRNA. Translation: AAB88005.1 .
    AF063658 mRNA. Translation: AAC16450.1 .
    AC021220 Genomic DNA. No translation available.
    AC111194 Genomic DNA. No translation available.
    BC131822 mRNA. Translation: AAI31823.1 .
    L04947 mRNA. Translation: AAA59459.1 .
    X61656 mRNA. Translation: CAA43837.1 .
    X89776 Genomic DNA. Translation: CAA61916.1 .
    CCDSi CCDS3497.1. [P35968-1 ]
    PIRi JC1402.
    RefSeqi NP_002244.1. NM_002253.2. [P35968-1 ]
    UniGenei Hs.479756.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VR2 X-ray 2.40 A 806-1171 [» ]
    1Y6A X-ray 2.10 A 806-1171 [» ]
    1Y6B X-ray 2.10 A 806-1171 [» ]
    1YWN X-ray 1.71 A 806-1171 [» ]
    2M59 NMR - A/B 759-795 [» ]
    2OH4 X-ray 2.05 A 806-1171 [» ]
    2P2H X-ray 1.95 A 815-1171 [» ]
    2P2I X-ray 2.40 A/B 815-1171 [» ]
    2QU5 X-ray 2.95 A 815-1171 [» ]
    2QU6 X-ray 2.10 A/B 815-1171 [» ]
    2RL5 X-ray 2.65 A 815-1171 [» ]
    2X1W X-ray 2.70 L/M/N/O 120-326 [» ]
    2X1X X-ray 3.10 R 120-326 [» ]
    2XIR X-ray 1.50 A 806-1171 [» ]
    3B8Q X-ray 2.75 A/B 815-1171 [» ]
    3B8R X-ray 2.70 A/B 815-1171 [» ]
    3BE2 X-ray 1.75 A 815-1171 [» ]
    3C7Q X-ray 2.10 A 806-1171 [» ]
    3CJF X-ray 2.15 A 806-1168 [» ]
    3CJG X-ray 2.25 A 806-1168 [» ]
    3CP9 X-ray 2.50 A/B 815-1171 [» ]
    3CPB X-ray 2.70 A/B 815-1171 [» ]
    3CPC X-ray 2.40 A/B 815-1171 [» ]
    3DTW X-ray 2.90 A/B 815-1171 [» ]
    3EFL X-ray 2.20 A/B 815-1171 [» ]
    3EWH X-ray 1.60 A 815-1171 [» ]
    3KVQ X-ray 2.70 A 657-764 [» ]
    3S35 X-ray 2.20 X 220-338 [» ]
    3S36 X-ray 3.20 X 220-338 [» ]
    3S37 X-ray 2.70 X 220-338 [» ]
    3U6J X-ray 2.15 A 815-1171 [» ]
    3V2A X-ray 3.20 R 2-764 [» ]
    3V6B X-ray 3.20 R 132-548 [» ]
    3VHE X-ray 1.55 A 811-1169 [» ]
    3VHK X-ray 2.49 A 806-1171 [» ]
    3VID X-ray 2.30 A 813-1168 [» ]
    3VNT X-ray 1.64 A 806-1171 [» ]
    3VO3 X-ray 1.52 A 806-1171 [» ]
    4AG8 X-ray 1.95 A 806-1171 [» ]
    4AGC X-ray 2.00 A 787-1171 [» ]
    4AGD X-ray 2.81 A 787-1171 [» ]
    4ASD X-ray 2.03 A 787-1171 [» ]
    4ASE X-ray 1.83 A 787-1171 [» ]
    ProteinModelPortali P35968.
    SMRi P35968. Positions 32-756, 759-795, 815-1209.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109992. 29 interactions.
    DIPi DIP-486N.
    IntActi P35968. 21 interactions.
    MINTi MINT-127732.
    STRINGi 9606.ENSP00000263923.

    Chemistry

    BindingDBi P35968.
    ChEMBLi CHEMBL2111428.
    DrugBanki DB00398. Sorafenib.
    DB01268. Sunitinib.
    GuidetoPHARMACOLOGYi 1813.

    PTM databases

    PhosphoSitei P35968.

    Polymorphism databases

    DMDMi 9087218.

    Proteomic databases

    PaxDbi P35968.
    PRIDEi P35968.

    Protocols and materials databases

    DNASUi 3791.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263923 ; ENSP00000263923 ; ENSG00000128052 . [P35968-1 ]
    GeneIDi 3791.
    KEGGi hsa:3791.
    UCSCi uc003has.3. human. [P35968-1 ]
    uc011bzx.2. human. [P35968-2 ]

    Organism-specific databases

    CTDi 3791.
    GeneCardsi GC04M055944.
    HGNCi HGNC:6307. KDR.
    HPAi CAB004028.
    MIMi 191306. gene.
    602089. phenotype.
    neXtProti NX_P35968.
    Orphaneti 91415. Familial capillary hemangioma.
    PharmGKBi PA30086.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG053432.
    InParanoidi P35968.
    KOi K05098.
    OMAi ISYAGMV.
    OrthoDBi EOG75F4CC.
    PhylomeDBi P35968.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_12473. Neurophilin interactions with VEGF and VEGFR.
    REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.
    REACT_13552. Integrin cell surface interactions.
    SignaLinki P35968.

    Miscellaneous databases

    EvolutionaryTracei P35968.
    GeneWikii Kinase_insert_domain_receptor.
    GenomeRNAii 3791.
    NextBioi 14887.
    PROi P35968.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35968.
    Bgeei P35968.
    CleanExi HS_KDR.
    Genevestigatori P35968.

    Family and domain databases

    Gene3Di 2.60.40.10. 8 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.
    IPR009136. VEGFR2_rcpt.
    [Graphical view ]
    PANTHERi PTHR24416:SF45. PTHR24416:SF45. 1 hit.
    Pfami PF07679. I-set. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    PRINTSi PR01834. VEGFRECEPTR2.
    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. "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 3), INTERACTION WITH VEGFC, SUBCELLULAR LOCATION.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INHIBITION OF LYMPHANGIOGENESIS, INTERACTION WITH VEGFC, TISSUE SPECIFICITY.
    3. "Full length human KDR/flk-1 sequence."
      Yin L.Y., Wu Y., Patterson C.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Coding region for human VEGF receptor KDR (VEGFR-2)."
      Yu Y., Whitney R.G., Sato J.D.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Umbilical vein.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1), VARIANT HIS-472.
    7. "Identification of a new endothelial cell growth factor receptor tyrosine kinase."
      Terman B.I., Carrion M.E., Kovacs E., Rasmussen B.A., Eddy R.L., Shows T.B.
      Oncogene 6:1677-1683(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-1356 (ISOFORM 1), VARIANT GLU-848.
      Tissue: Umbilical vein.
    8. "Cloning and functional analysis of the promoter for KDR/flk-1, a receptor for vascular endothelial growth factor."
      Patterson C., Perrella M.A., Hsieh C.-M., Yoshizumi M., Lee M.-E., Harber E.
      J. Biol. Chem. 270:23111-23118(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    9. "Identification of the KDR tyrosine kinase as a receptor for vascular endothelial cell growth factor."
      Terman B.I., Dougher-Vermazen M., Carrion M.E., Dimitrov D., Armellino D.C., Gospodarowicz D., Boehlen P.
      Biochem. Biophys. Res. Commun. 187:1579-1586(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VEGFA.
    10. "Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor."
      Waltenberger J., Claesson-Welsh L., Siegbahn A., Shibuya M., Heldin C.H.
      J. Biol. Chem. 269:26988-26995(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS VEGFA RECEPTOR; IN REGULATION OF CELL SHAPE; ACTIN CYTOSKELETON REORGANIZATION; CELL MIGRATION AND CELL PROLIFERATION, AUTOPHOSPHORYLATION.
    11. "The 230 kDa mature form of KDR/Flk-1 (VEGF receptor-2) activates the PLC-gamma pathway and partially induces mitotic signals in NIH3T3 fibroblasts."
      Takahashi T., Shibuya M.
      Oncogene 14:2079-2089(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN VEGFA SIGNALING; PHOSPHORYLATION OF PLCG1; ACTIVATION OF MAP KINASES AND IN PROMOTING PROLIFERATION OF ENDOTHELIAL CELLS, INTERACTION WITH VEGFA AND PLCG1, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, GLYCOSYLATION.
    12. "VEGF-A induces expression of eNOS and iNOS in endothelial cells via VEGF receptor-2 (KDR)."
      Kroll J., Waltenberger J.
      Biochem. Biophys. Res. Commun. 252:743-746(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INDUCTION OF NOS2 AND NOS3.
    13. "Vascular endothelial growth factor regulates endothelial cell survival through the phosphatidylinositol 3'-kinase/Akt signal transduction pathway. Requirement for Flk-1/KDR activation."
      Gerber H.P., McMurtrey A., Kowalski J., Yan M., Keyt B.A., Dixit V., Ferrara N.
      J. Biol. Chem. 273:30336-30343(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF THE PHOSPHATIDYLINOSITOL 3-KINASE AND AKT1 SIGNALING PATHWAY.
    14. "A novel function of VEGF receptor-2 (KDR): rapid release of nitric oxide in response to VEGF-A stimulation in endothelial cells."
      Kroll J., Waltenberger J.
      Biochem. Biophys. Res. Commun. 265:636-639(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NITRIC OXIDE RELEASE.
    15. "Vascular endothelial growth factor receptor KDR tyrosine kinase activity is increased by autophosphorylation of two activation loop tyrosine residues."
      Kendall R.L., Rutledge R.Z., Mao X., Tebben A.J., Hungate R.W., Thomas K.A.
      J. Biol. Chem. 274:6453-6460(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT GLU-848, PHOSPHORYLATION AT TYR-1054 AND TYR-1059, ENZYME REGULATION.
    16. "Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization."
      Dougher M., Terman B.I.
      Oncogene 18:1619-1627(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG1 AND PTK2/FAK1, INTERACTION WITH VEGFA, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-996; TYR-1054 AND TYR-1059, MUTAGENESIS OF TYR-996; TYR-1054 AND TYR-1059, SUBCELLULAR LOCATION, ENZYME REGULATION.
    17. "Identification of specific molecular structures of human immunodeficiency virus type 1 Tat relevant for its biological effects on vascular endothelial cells."
      Mitola S., Soldi R., Zanon I., Barra L., Gutierrez M.I., Berkhout B., Giacca M., Bussolino F.
      J. Virol. 74:344-353(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    18. "A single autophosphorylation site on KDR/Flk-1 is essential for VEGF-A-dependent activation of PLC-gamma and DNA synthesis in vascular endothelial cells."
      Takahashi T., Yamaguchi S., Chida K., Shibuya M.
      EMBO J. 20:2768-2778(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOTHELIAL CELL PROLIFERATION; PHOSPHORYLATION OF PLCG1 AND ACTIVATION OF MAP KINASES, PHOSPHORYLATION AT TYR-1175 AND TYR-1214, MUTAGENESIS OF LYS-868 AND TYR-1175.
    19. "Vascular endothelial growth factor-dependent down-regulation of Flk-1/KDR involves Cbl-mediated ubiquitination. Consequences on nitric oxide production from endothelial cells."
      Duval M., Bedard-Goulet S., Delisle C., Gratton J.P.
      J. Biol. Chem. 278:20091-20097(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, FUNCTION IN NITRIC OXIDE PRODUCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBL.
    20. "Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-3) heterodimerization with VEGFR-2 in primary lymphatic endothelial cells regulates tyrosine phosphorylation sites."
      Dixelius J., Makinen T., Wirzenius M., Karkkainen M.J., Wernstedt C., Alitalo K., Claesson-Welsh L.
      J. Biol. Chem. 278:40973-40979(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT4.
    21. "The adaptor protein shb binds to tyrosine 1175 in vascular endothelial growth factor (VEGF) receptor-2 and regulates VEGF-dependent cellular migration."
      Holmqvist K., Cross M.J., Rolny C., Haegerkvist R., Rahimi N., Matsumoto T., Claesson-Welsh L., Welsh M.
      J. Biol. Chem. 279:22267-22275(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB, FUNCTION IN CELL MIGRATION.
    22. "Phosphorylated KDR is expressed in the neoplastic and stromal elements of human renal tumours and shuttles from cell membrane to nucleus."
      Fox S.B., Turley H., Cheale M., Blazquez C., Roberts H., James N., Cook N., Harris A., Gatter K.
      J. Pathol. 202:313-320(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    23. "Vascular endothelial growth factor (VEGF)-D and VEGF-A differentially regulate KDR-mediated signaling and biological function in vascular endothelial cells."
      Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.
      J. Biol. Chem. 279:36148-36157(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VEGFA AND VEGFD, PHOSPHORYLATION AT TYR-1054 AND TYR-1059, FUNCTION IN VEGFA AND VEGFD SIGNALING; ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1; ACTIVATION OF AKT1; PHOSPHORYLATION OF PLCG1 AND NOS3; MODULATION OF INTRACELLULAR CA(2+) LEVELS; CELL SURVIVAL AND POSITIVE REGULATION OF CELL PROLIFERATION; CELL MIGRATION AND ANGIOGENESIS, ENZYME REGULATION.
    24. Cited for: FUNCTION IN CELL MIGRATION; PHOSPHORYLATION OF PLCG1; ACTIVATION OF MAPK1/ERK2; MAPK3/ERK1 AND THE MAP KINASES AND IN REGULATION OF ACTIN CYTOSKELETON REORGANIZATION, INTERACTION WITH SH2D2A/TSAD, PHOSPHORYLATION AT TYR-951; TYR-1054; TYR-1059; TYR-1214; TYR-1305; TYR-1309 AND TYR-1319, MUTAGENESIS OF TYR-951.
    25. "Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of Nck and activation of Fyn leading to SAPK2/p38 activation and endothelial cell migration in response to VEGF."
      Lamalice L., Houle F., Huot J.
      J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ENDOTHELIAL CELL MIGRATION; ACTIVATION OF MAP KINASES AND IN PHOSPHORYLATION OF FYN; SRC AND NCK1, INTERACTION WITH GRB2; FYN AND NCK1, MUTAGENESIS OF TYR-1214.
    26. "Intrinsic tyrosine kinase activity is required for vascular endothelial growth factor receptor 2 ubiquitination, sorting and degradation in endothelial cells."
      Ewan L.C., Jopling H.M., Jia H., Mittar S., Bagherzadeh A., Howell G.J., Walker J.H., Zachary I.C., Ponnambalam S.
      Traffic 7:1270-1282(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, DEGRADATION.
    27. "Phosphorylation of tyrosine 801 of vascular endothelial growth factor receptor-2 is necessary for Akt-dependent endothelial nitric-oxide synthase activation and nitric oxide release from endothelial cells."
      Blanes M.G., Oubaha M., Rautureau Y., Gratton J.P.
      J. Biol. Chem. 282:10660-10669(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF AKT1; PHOSPHORYLATION OF PLCG1 AND NOS3 AND REGULATION OF NITRIC OXIDE PRODUCTION, PHOSPHORYLATION AT TYR-801, MUTAGENESIS OF TYR-801.
    28. "AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice."
      Zhang H., He Y., Dai S., Xu Z., Luo Y., Wan T., Luo D., Jones D., Tang S., Chen H., Sessa W.C., Min W.
      J. Clin. Invest. 118:3904-3916(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP.
    29. "Transcriptional profiling reveals a critical role for tyrosine phosphatase VE-PTP in regulation of VEGFR2 activity and endothelial cell morphogenesis."
      Mellberg S., Dimberg A., Bahram F., Hayashi M., Rennel E., Ameur A., Westholm J.O., Larsson E., Lindahl P., Cross M.J., Claesson-Welsh L.
      FASEB J. 23:1490-1502(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-951; TYR-1175 AND TYR-1214, DEPHOSPHORYLATION BY PTPRB.
    30. "New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival."
      Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.
      Mol. Cell. Biol. 29:241-253(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-801; TYR-951; TYR-996; TYR-1054; TYR-1059; TYR-1175 AND TYR-1214; DEPHOSPHORYLATION AT TYR-951; TYR-996; TYR-1054; TYR-1059; TYR-1175 AND TYR-1214 BY PTPRJ.
    31. "VEGF-dependent tumor angiogenesis requires inverse and reciprocal regulation of VEGFR1 and VEGFR2."
      Zhang Z., Neiva K.G., Lingen M.W., Ellis L.M., Nor J.E.
      Cell Death Differ. 17:499-512(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS VEGFA RECEPTOR IN TUMOR ANGIOGENESIS, SUBCELLULAR LOCATION, UBIQUITINATION.
    32. "Neuroblastoma progression correlates with downregulation of the lymphangiogenesis inhibitor sVEGFR-2."
      Becker J., Pavlakovic H., Ludewig F., Wilting F., Weich H.A., Albuquerque R., Ambati J., Wilting J.
      Clin. Cancer Res. 16:1431-1441(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LYMPHANGIOGENESIS (ISOFORM 2).
    33. Cited for: INTERACTION WITH VEGFC AND FLT4, SUBCELLULAR LOCATION, FUNCTION IN ANGIOGENESIS.
    34. "The VEGFR2 receptor tyrosine kinase undergoes constitutive endosome-to-plasma membrane recycling."
      Jopling H.M., Howell G.J., Gamper N., Ponnambalam S.
      Biochem. Biophys. Res. Commun. 410:170-176(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    35. "Blood vessel endothelial VEGFR-2 delays lymphangiogenesis: an endogenous trapping mechanism links lymph- and angiogenesis."
      Nakao S., Zandi S., Hata Y., Kawahara S., Arita R., Schering A., Sun D., Melhorn M.I., Ito Y., Lara-Castillo N., Ishibashi T., Hafezi-Moghadam A.
      Blood 117:1081-1090(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LYMPHANGIOGENESIS, INTERACTION WITH FLT4 AND VEGFC.
    36. "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 ROLE IN ANGIOGENESIS.
    37. "Vascular endothelial growth factor receptor-2: structure, function, intracellular signalling and therapeutic inhibition."
      Holmes K., Roberts O.L., Thomas A.M., Cross M.J.
      Cell. Signal. 19:2003-2012(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    38. "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.
    39. "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.
    40. "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.
    41. "Vascular endothelial growth factor receptor-2 in breast cancer."
      Guo S., Colbert L.S., Fuller M., Zhang Y., Gonzalez-Perez R.R.
      Biochim. Biophys. Acta 1806:108-121(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
    42. "Tyrosine kinase receptor Flt/VEGFR family: its characterization related to angiogenesis and cancer."
      Shibuya M.
      Genes Cancer 1:1119-1123(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN ANGIOGENESIS AND CANCER.
    43. "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.
    44. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-982 AND SER-984, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    45. "Programmed cell death 6 (PDCD6) inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of VEGFR-2."
      Rho S.B., Song Y.J., Lim M.C., Lee S.H., Kim B.R., Park S.Y.
      Cell. Signal. 24:131-139(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PDCD6.
    46. "VEGFR2 functions as an H(2)S-targeting receptor protein kinase with its novel Cys1045-Cys1024 disulfide bond serving as a specific molecular switch for hydrogen sulfide actions in vascular endothelial cells."
      Tao B.B., Liu S.Y., Zhang C.C., Fu W., Cai W.J., Wang Y., Shen Q., Wang M.J., Chen Y., Zhang L.J., Zhu Y.Z., Zhu Y.C.
      Antioxid. Redox Signal. 19:448-464(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, REDOX-ACTIVE DISULFIDE BOND, MUTAGENESIS OF CYS-1045.
    47. "Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis."
      McTigue M.A., Wickersham J.A., Pinko C., Showalter R.E., Parast C.V., Tempczyk-Russell A., Gehring M.R., Mroczkowski B., Kan C.-C., Villafranca J.E., Appelt K.
      Structure 7:319-330(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 806-1171, FUNCTION, PHOSPHORYLATION AT TYR-1059, IDENTIFICATION BY MASS SPECTROMETRY.
    48. Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 806-1171 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    49. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 815-1171 IN COMPLEX WITH SYNTHETIC INHIBITOR.
    50. "Design, synthesis, and biological evaluation of novel 3-aryl-4-(1H-indole-3yl)-1,5-dihydro-2H-pyrrole-2-ones as vascular endothelial growth factor receptor (VEGF-R) inhibitors."
      Peifer C., Selig R., Kinkel K., Ott D., Totzke F., Schaechtele C., Heidenreich R., Roecken M., Schollmeyer D., Laufer S.
      J. Med. Chem. 51:3814-3824(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 806-1171 IN COMPLEX WITH SYNTHETIC INHIBITOR, FUNCTION.
    51. "Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling."
      Yang Y., Xie P., Opatowsky Y., Schlessinger J.
      Proc. Natl. Acad. Sci. U.S.A. 107:1906-1911(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 657-764, SUBUNIT, AUTOPHOSPHORYLATION, FUNCTION IN VEGFA SIGNALING AND ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1, MUTAGENESIS OF ARG-726 AND ASP-731.
    52. Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 120-326 IN COMPLEX WITH VEGFC, INTERACTION WITH VEGFC, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-143; ASN-245 AND ASN-318.
    53. "The structural basis for the function of two anti-VEGF receptor 2 antibodies."
      Franklin M.C., Navarro E.C., Wang Y., Patel S., Singh P., Zhang Y., Persaud K., Bari A., Griffith H., Shen L., Balderes P., Kussie P.
      Structure 19:1097-1107(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 220-338 IN COMPLEX WITH ANTIBODY FRAGMENT, DISULFIDE BOND, GLYCOSYLATION AT ASN-245 AND ASN-318.
    54. "Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma."
      Walter J.W., North P.E., Waner M., Mizeracki A., Blei F., Walker J.W.T., Reinisch J.F., Marchuk D.A.
      Genes Chromosomes Cancer 33:295-303(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCI SER-1147.
    55. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-275 AND ARG-873.
    56. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-2; MET-136; GLY-248; ILE-297; VAL-462; HIS-472; ARG-482; ARG-539; MET-689; ASN-814 AND THR-1065.
    57. "Suppressed NFAT-dependent VEGFR1 expression and constitutive VEGFR2 signaling in infantile hemangioma."
      Jinnin M., Medici D., Park L., Limaye N., Liu Y., Boscolo E., Bischoff J., Vikkula M., Boye E., Olsen B.R.
      Nat. Med. 14:1236-1246(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCI SUSCEPTIBILITY ARG-482.

    Entry informationi

    Entry nameiVGFR2_HUMAN
    AccessioniPrimary (citable) accession number: P35968
    Secondary accession number(s): A2RRS0
    , B5A925, C5IFA0, O60723, Q14178
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 169 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3