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P35968

- VGFR2_HUMAN

UniProt

P35968 - VGFR2_HUMAN

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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

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 tyrosine kinase activity Source: UniProtKB
  6. receptor signaling protein tyrosine kinase activity Source: BHF-UCL
  7. transmembrane receptor protein tyrosine kinase activity Source: BHF-UCL
  8. vascular endothelial growth factor-activated receptor activity Source: UniProtKB
  9. 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
Complete GO annotation...

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 vesicle Source: UniProtKB-KW
  3. early endosome Source: BHF-UCL
  4. endosome Source: UniProtKB
  5. external side of plasma membrane Source: Ensembl
  6. extracellular region Source: UniProtKB-KW
  7. Golgi apparatus Source: UniProtKB
  8. integral component of plasma membrane Source: UniProtKB
  9. membrane raft Source: UniProtKB
  10. nucleus Source: UniProtKB-KW
  11. plasma membrane Source: UniProtKB
  12. sorting endosome Source: BHF-UCL
Complete GO annotation...

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...)1 Publication
Disulfide bondi150 ↔ 200
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)2 Publications
Disulfide bondi246 ↔ 307
Glycosylationi318 – 3181N-linked (GlcNAc...)2 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 – 8011Phosphotyrosine2 Publications
Modified residuei951 – 9511Phosphotyrosine; by autocatalysis3 Publications
Modified residuei982 – 9821Phosphoserine1 Publication
Modified residuei984 – 9841Phosphoserine1 Publication
Modified residuei996 – 9961Phosphotyrosine; by autocatalysis2 Publications
Disulfide bondi1024 ↔ 1045Redox-active
Modified residuei1054 – 10541Phosphotyrosine; by autocatalysis5 Publications
Modified residuei1059 – 10591Phosphotyrosine; by autocatalysis6 Publications
Modified residuei1175 – 11751Phosphotyrosine; by autocatalysis3 Publications
Modified residuei1214 – 12141Phosphotyrosine; by autocatalysis4 Publications
Modified residuei1305 – 13051Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1309 – 13091Phosphotyrosine; by autocatalysis1 Publication
Modified residuei1319 – 13191Phosphotyrosine; by autocatalysis1 Publication

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

BgeeiP35968.
CleanExiHS_KDR.
ExpressionAtlasiP35968. baseline and differential.
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
HSPG2P981605EBI-1005487,EBI-947664
ITGA2P173012EBI-1005487,EBI-702960
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
VEGFAP15692-46EBI-1005487,EBI-1026691

Protein-protein interaction databases

BioGridi109992. 29 interactions.
DIPiDIP-486N.
IntActiP35968. 22 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[»]
2METNMR-A/B/C759-795[»]
2MEUNMR-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.
GeneTreeiENSGT00760000118923.
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

        10         20         30         40         50
MQSKVLLAVA LWLCVETRAA SVGLPSVSLD LPRLSIQKDI LTIKANTTLQ
60 70 80 90 100
ITCRGQRDLD WLWPNNQSGS EQRVEVTECS DGLFCKTLTI PKVIGNDTGA
110 120 130 140 150
YKCFYRETDL ASVIYVYVQD YRSPFIASVS DQHGVVYITE NKNKTVVIPC
160 170 180 190 200
LGSISNLNVS LCARYPEKRF VPDGNRISWD SKKGFTIPSY MISYAGMVFC
210 220 230 240 250
EAKINDESYQ SIMYIVVVVG YRIYDVVLSP SHGIELSVGE KLVLNCTART
260 270 280 290 300
ELNVGIDFNW EYPSSKHQHK KLVNRDLKTQ SGSEMKKFLS TLTIDGVTRS
310 320 330 340 350
DQGLYTCAAS SGLMTKKNST FVRVHEKPFV AFGSGMESLV EATVGERVRI
360 370 380 390 400
PAKYLGYPPP EIKWYKNGIP LESNHTIKAG HVLTIMEVSE RDTGNYTVIL
410 420 430 440 450
TNPISKEKQS HVVSLVVYVP PQIGEKSLIS PVDSYQYGTT QTLTCTVYAI
460 470 480 490 500
PPPHHIHWYW QLEEECANEP SQAVSVTNPY PCEEWRSVED FQGGNKIEVN
510 520 530 540 550
KNQFALIEGK NKTVSTLVIQ AANVSALYKC EAVNKVGRGE RVISFHVTRG
560 570 580 590 600
PEITLQPDMQ PTEQESVSLW CTADRSTFEN LTWYKLGPQP LPIHVGELPT
610 620 630 640 650
PVCKNLDTLW KLNATMFSNS TNDILIMELK NASLQDQGDY VCLAQDRKTK
660 670 680 690 700
KRHCVVRQLT VLERVAPTIT GNLENQTTSI GESIEVSCTA SGNPPPQIMW
710 720 730 740 750
FKDNETLVED SGIVLKDGNR NLTIRRVRKE DEGLYTCQAC SVLGCAKVEA
760 770 780 790 800
FFIIEGAQEK TNLEIIILVG TAVIAMFFWL LLVIILRTVK RANGGELKTG
810 820 830 840 850
YLSIVMDPDE LPLDEHCERL PYDASKWEFP RDRLKLGKPL GRGAFGQVIE
860 870 880 890 900
ADAFGIDKTA TCRTVAVKML KEGATHSEHR ALMSELKILI HIGHHLNVVN
910 920 930 940 950
LLGACTKPGG PLMVIVEFCK FGNLSTYLRS KRNEFVPYKT KGARFRQGKD
960 970 980 990 1000
YVGAIPVDLK RRLDSITSSQ SSASSGFVEE KSLSDVEEEE APEDLYKDFL
1010 1020 1030 1040 1050
TLEHLICYSF QVAKGMEFLA SRKCIHRDLA ARNILLSEKN VVKICDFGLA
1060 1070 1080 1090 1100
RDIYKDPDYV RKGDARLPLK WMAPETIFDR VYTIQSDVWS FGVLLWEIFS
1110 1120 1130 1140 1150
LGASPYPGVK IDEEFCRRLK EGTRMRAPDY TTPEMYQTML DCWHGEPSQR
1160 1170 1180 1190 1200
PTFSELVEHL GNLLQANAQQ DGKDYIVLPI SETLSMEEDS GLSLPTSPVS
1210 1220 1230 1240 1250
CMEEEEVCDP KFHYDNTAGI SQYLQNSKRK SRPVSVKTFE DIPLEEPEVK
1260 1270 1280 1290 1300
VIPDDNQTDS GMVLASEELK TLEDRTKLSP SFGGMVPSKS RESVASEGSN
1310 1320 1330 1340 1350
QTSGYQSGYH SDDTDTTVYS SEEAELLKLI EIGVQTGSTA QILQPDSGTT

LSSPPV
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 [» ]
2MET NMR - A/B/C 759-795 [» ]
2MEU 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. 22 interactions.
MINTi MINT-127732.
STRINGi 9606.ENSP00000263923.

Chemistry

BindingDBi P35968.
ChEMBLi CHEMBL2111336.
DrugBanki DB06626. Axitinib.
DB08875. Cabozantinib.
DB06589. Pazopanib.
DB08901. Ponatinib.
DB08896. Regorafenib.
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.
GeneTreei ENSGT00760000118923.
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

Bgeei P35968.
CleanExi HS_KDR.
ExpressionAtlasi P35968. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 170 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