UniProtKB - P35968 (VGFR2_HUMAN)
Vascular endothelial growth factor receptor 2
KDR
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.
23 PublicationsCatalytic activityi
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]PROSITE-ProRule annotation2 PublicationsEC:2.7.10.1PROSITE-ProRule annotation2 Publications
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 868 | ATPCurated | 1 | |
Active sitei | 1028 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 840 – 848 | ATPCurated | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cadherin binding Source: UniProtKB
- growth factor binding Source: BHF-UCL
- Hsp90 protein binding Source: BHF-UCL
- identical protein binding Source: IntAct
- integrin binding Source: BHF-UCL
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein tyrosine kinase activity Source: UniProtKB
- transmembrane receptor protein tyrosine kinase activity Source: GO_Central
- vascular endothelial growth factor-activated receptor activity Source: UniProtKB
- vascular endothelial growth factor binding Source: BHF-UCL
GO - Biological processi
- angiogenesis Source: GO_Central
- branching involved in blood vessel morphogenesis Source: BHF-UCL
- calcium ion homeostasis Source: Ensembl
- calcium-mediated signaling using intracellular calcium source Source: UniProtKB
- cell fate commitment Source: Ensembl
- cell maturation Source: Ensembl
- cell migration Source: GO_Central
- cell migration involved in sprouting angiogenesis Source: BHF-UCL
- cellular response to hydrogen sulfide Source: BHF-UCL
- cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
- embryonic hemopoiesis Source: UniProtKB
- endocardium development Source: Ensembl
- endothelial cell differentiation Source: GO_Central
- endothelium development Source: UniProtKB
- ERK1 and ERK2 cascade Source: BHF-UCL
- hematopoietic progenitor cell differentiation Source: GO_Central
- lung alveolus development Source: Ensembl
- lymph vessel development Source: Ensembl
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of endothelial cell apoptotic process Source: UniProtKB
- negative regulation of gene expression Source: BHF-UCL
- ovarian follicle development Source: Ensembl
- peptidyl-tyrosine autophosphorylation Source: BHF-UCL
- peptidyl-tyrosine phosphorylation Source: UniProtKB
- positive regulation of angiogenesis Source: UniProtKB
- positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
- positive regulation of BMP signaling pathway Source: Ensembl
- positive regulation of cell migration Source: BHF-UCL
- positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
- positive regulation of cell population proliferation Source: BHF-UCL
- positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
- positive regulation of endothelial cell migration Source: BHF-UCL
- positive regulation of endothelial cell proliferation Source: UniProtKB
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
- positive regulation of focal adhesion assembly Source: BHF-UCL
- positive regulation of kinase activity Source: GO_Central
- positive regulation of macroautophagy Source: MGI
- positive regulation of MAPK cascade Source: UniProtKB
- positive regulation of mesenchymal cell proliferation Source: Ensembl
- positive regulation of mitochondrial depolarization Source: MGI
- positive regulation of mitochondrial fission Source: MGI
- positive regulation of nitric-oxide synthase biosynthetic process Source: UniProtKB
- positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
- positive regulation of positive chemotaxis Source: BHF-UCL
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of vasculogenesis Source: UniProtKB
- post-embryonic camera-type eye morphogenesis Source: Ensembl
- protein autophosphorylation Source: UniProtKB
- protein kinase B signaling Source: BHF-UCL
- regulation of bone development Source: Ensembl
- regulation of cell shape Source: BHF-UCL
- regulation of hematopoietic progenitor cell differentiation Source: Ensembl
- surfactant homeostasis Source: Ensembl
- transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
- vascular endothelial growth factor receptor-2 signaling pathway Source: BHF-UCL
- vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
- vascular endothelial growth factor signaling pathway Source: BHF-UCL
- vascular wound healing Source: BHF-UCL
- vasculogenesis Source: UniProtKB
Keywordsi
Molecular function | Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase |
Biological process | Angiogenesis, Differentiation, Host-virus interaction |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.10.1, 2681 |
PathwayCommonsi | P35968 |
Reactomei | R-HSA-194306, Neurophilin interactions with VEGF and VEGFR R-HSA-195399, VEGF binds to VEGFR leading to receptor dimerization R-HSA-216083, Integrin cell surface interactions R-HSA-4420097, VEGFA-VEGFR2 Pathway R-HSA-5218921, VEGFR2 mediated cell proliferation R-HSA-9673768, Signaling by membrane-tethered fusions of PDGFRA or PDGFRB |
SignaLinki | P35968 |
SIGNORi | P35968 |
Names & Taxonomyi
Protein namesi | Recommended name: Vascular endothelial growth factor receptor 2Curated (EC:2.7.10.12 Publications)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 | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:6307, KDR |
MIMi | 191306, gene |
neXtProti | NX_P35968 |
VEuPathDBi | HostDB:ENSG00000128052 |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum 1 Publication
Other locations
- Cell junction By similarity
Note: Localized with RAP1A at cell-cell junctions (By similarity). Colocalizes with ERN1 and XBP1 in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (PubMed:23529610).By similarity1 Publication
Endosome
Nucleus
Plasma membrane
Cytoplasm and Cytosol
Other locations
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.
Extracellular region or secreted
- Secreted Curated
Extracellular region or secreted
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Endosome
- early endosome Source: BHF-UCL
- endosome Source: UniProtKB
- sorting endosome Source: BHF-UCL
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Golgi apparatus
- Golgi apparatus Source: UniProtKB
Nucleus
- nucleus Source: UniProtKB-SubCell
Plasma Membrane
- external side of plasma membrane Source: Ensembl
- integral component of plasma membrane Source: UniProtKB
- plasma membrane Source: UniProtKB
Other locations
- cell junction Source: UniProtKB
- membrane raft Source: UniProtKB
- receptor complex Source: GO_Central
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 20 – 764 | ExtracellularSequence analysisAdd BLAST | 745 | |
Transmembranei | 765 – 785 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 786 – 1356 | CytoplasmicSequence analysisAdd BLAST | 571 |
Keywords - Cellular componenti
Cell junction, Cell membrane, Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Membrane, Nucleus, SecretedPathology & Biotechi
Involvement in diseasei
Hemangioma, capillary infantile (HCI)3 Publications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_042057 | 482 | C → R in HCI; associated with disease 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 PublicationsCorresponds to variant dbSNP:rs34231037EnsemblClinVar. | 1 | |
Natural variantiVAR_063147 | 1147 | P → S in HCI; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121917766EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 726 | R → A: Strongly reduced autophosphorylation and activation of MAP kinases. 1 Publication | 1 | |
Mutagenesisi | 731 | D → A: Strongly reduced autophosphorylation and activation of MAP kinases. 1 Publication | 1 | |
Mutagenesisi | 801 | Y → F: Abolishes stimulation of nitric oxide synthesis. 1 Publication | 1 | |
Mutagenesisi | 868 | K → M: Loss of enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 951 | Y → F: Abolishes reorganization of the actin cytoskeleton and cell migration in response to VEGFA. 1 Publication | 1 | |
Mutagenesisi | 996 | Y → F: Strongly reduced autophosphorylation. Reduces phosphorylation of PLCG1. 1 Publication | 1 | |
Mutagenesisi | 1045 | C → A: Significantly higher kinase activity. 1 Publication | 1 | |
Mutagenesisi | 1054 | Y → F: Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1059. 1 Publication | 1 | |
Mutagenesisi | 1059 | Y → F: Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1054. 1 Publication | 1 | |
Mutagenesisi | 1175 | Y → F: Abolishes phosphorylation of PLCG1 and MAP kinases in response to VEGFA. 1 Publication | 1 | |
Mutagenesisi | 1214 | Y → F: Loss of phosphorylation site. Abolishes reorganization of the actin cytoskeleton in response to VEGFA. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 3791 |
MalaCardsi | KDR |
MIMi | 602089, phenotype |
OpenTargetsi | ENSG00000128052 |
Orphaneti | 464293, NON RARE IN EUROPE: Infantile capillary hemangioma 3303, Tetralogy of Fallot |
PharmGKBi | PA30086 |
Miscellaneous databases
Pharosi | P35968, Tclin |
Chemistry databases
ChEMBLi | CHEMBL279 |
DrugBanki | DB04727, 1-{4-[4-Amino-6-(4-methoxyphenyl)furo[2,3-d]pyrimidin-5-yl]phenyl}-3-[2-fluoro-5-(trifluoromethyl)phenyl]urea DB07514, 3-(2-aminoquinazolin-6-yl)-1-(3,3-dimethylindolin-6-yl)-4-methylpyridin-2(1H)-one DB07528, 3-(2-aminoquinazolin-6-yl)-4-methyl-1-[3-(trifluoromethyl)phenyl]pyridin-2(1H)-one DB06938, 4-[[2-[[4-chloro-3-(trifluoromethyl)phenyl]amino]-3H-benzimidazol-5-yl]oxy]-N-methyl-pyridine-2-carboxamide DB07326, 6-chloro-N-pyrimidin-5-yl-3-{[3-(trifluoromethyl)phenyl]amino}-1,2-benzisoxazole-7-carboxamide DB06626, Axitinib DB08875, Cabozantinib DB04849, Cediranib DB05198, CYC116 DB12147, Erdafitinib DB12307, Foretinib DB12010, Fostamatinib DB06101, IMC-1C11 DB09078, Lenvatinib DB06080, Linifanib DB06595, Midostaurin DB07537, N'-(6-aminopyridin-3-yl)-N-(2-cyclopentylethyl)-4-methyl-benzene-1,3-dicarboxamide DB07183, N-(4-phenoxyphenyl)-2-[(pyridin-4-ylmethyl)amino]nicotinamide DB07333, N-(CYCLOPROPYLMETHYL)-4-(METHYLOXY)-3-({5-[3-(3-PYRIDINYL)PHENYL]-1,3-OXAZOL-2-YL}AMINO)BENZENESULFONAMIDE DB07334, N-[5-(ETHYLSULFONYL)-2-METHOXYPHENYL]-5-[3-(2-PYRIDINYL)PHENYL]-1,3-OXAZOL-2-AMINE DB07274, N-cyclopropyl-6-[(6,7-dimethoxyquinolin-4-yl)oxy]naphthalene-1-carboxamide DB09079, Nintedanib DB08519, N~4~-(3-methyl-1H-indazol-6-yl)-N~2~-(3,4,5-trimethoxyphenyl)pyrimidine-2,4-diamine DB08042, N~4~-methyl-N~4~-(3-methyl-1H-indazol-6-yl)-N~2~-(3,4,5-trimethoxyphenyl)pyrimidine-2,4-diamine DB06589, Pazopanib DB05931, Pegdinetanib DB08901, Ponatinib DB15822, Pralsetinib DB05984, RAF-265 DB05578, Ramucirumab DB08896, Regorafenib DB14840, Ripretinib DB06436, Semaxanib DB00398, Sorafenib DB01268, Sunitinib DB05075, TG-100801 DB11800, Tivozanib DB04879, Vatalanib DB05146, XL820 DB05014, XL999 |
DrugCentrali | P35968 |
GuidetoPHARMACOLOGYi | 1813 |
Genetic variation databases
BioMutai | KDR |
DMDMi | 9087218 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 19 | Sequence analysisAdd BLAST | 19 | |
ChainiPRO_0000016771 | 20 – 1356 | Vascular endothelial growth factor receptor 2Add BLAST | 1337 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 46 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 53 ↔ 103 | PROSITE-ProRule annotation | ||
Glycosylationi | 66 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 96 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 143 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 150 ↔ 200 | |||
Glycosylationi | 158 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 245 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 246 ↔ 307 | |||
Glycosylationi | 318 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 374 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 395 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 445 ↔ 530 | PROSITE-ProRule annotation | ||
Glycosylationi | 511 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 523 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 571 ↔ 642 | PROSITE-ProRule annotation | ||
Glycosylationi | 580 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 613 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 619 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 631 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 675 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 688 ↔ 737 | PROSITE-ProRule annotation | ||
Glycosylationi | 704 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 721 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 801 | Phosphotyrosine2 Publications | 1 | |
Modified residuei | 951 | Phosphotyrosine; by autocatalysis3 Publications | 1 | |
Modified residuei | 982 | PhosphoserineCombined sources | 1 | |
Modified residuei | 984 | PhosphoserineCombined sources | 1 | |
Modified residuei | 996 | Phosphotyrosine; by autocatalysis2 Publications | 1 | |
Disulfide bondi | 1024 ↔ 1045 | Redox-active | ||
Modified residuei | 1054 | Phosphotyrosine; by autocatalysis5 Publications | 1 | |
Modified residuei | 1059 | Phosphotyrosine; by autocatalysis6 Publications | 1 | |
Modified residuei | 1175 | Phosphotyrosine; by autocatalysis3 Publications | 1 | |
Modified residuei | 1214 | Phosphotyrosine; by autocatalysis4 Publications | 1 | |
Modified residuei | 1231 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1235 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1238 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1305 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
Modified residuei | 1309 | Phosphotyrosine; by autocatalysis1 Publication | 1 | |
Modified residuei | 1319 | Phosphotyrosine; by autocatalysis1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | P35968 |
jPOSTi | P35968 |
MassIVEi | P35968 |
MaxQBi | P35968 |
PaxDbi | P35968 |
PeptideAtlasi | P35968 |
PRIDEi | P35968 |
ProteomicsDBi | 55169 [P35968-1] 55170 [P35968-2] 55171 [P35968-3] |
PTM databases
CarbonylDBi | P35968 |
GlyGeni | P35968, 20 sites, 1 O-linked glycan (1 site) |
iPTMneti | P35968 |
PhosphoSitePlusi | P35968 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000128052, Expressed in placenta and 219 other tissues |
ExpressionAtlasi | P35968, baseline and differential |
Genevisiblei | P35968, HS |
Organism-specific databases
HPAi | ENSG00000128052, Low tissue specificity |
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 KDR/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 (via C-terminus domain) with ERN1 (via kinase domain); the interaction is facilitated in a XBP1 isoform 1- and vascular endothelial growth factor (VEGF)-dependent manner in endothelial cells (PubMed:23529610).
Interacts (via juxtamembrane region) with chaperone PDCL3 (via thioredoxin fold region); the interaction leads to increased KDR/VEGFR2 abundance through inhibition of its ubiquitination and degradation (PubMed:23792958, PubMed:26059764).
Interacts (tyrosine phosphorylated) with CCDC88A/GIV (via SH2-like region); binding requires autophosphorylation of the KDR/VEGFR2 C-terminal region (PubMed:25187647).
Interacts with isoform 2 of BSG (PubMed:25825981).
26 Publications(Microbial infection) Interacts with HIV-1 Tat.
1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 1175 | Interaction with SHBBy similarity | 1 |
Binary interactionsi
P35968
GO - Molecular functioni
- cadherin binding Source: UniProtKB
- growth factor binding Source: BHF-UCL
- Hsp90 protein binding Source: BHF-UCL
- identical protein binding Source: IntAct
- integrin binding Source: BHF-UCL
- vascular endothelial growth factor binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 109992, 77 interactors |
CORUMi | P35968 |
DIPi | DIP-486N |
IntActi | P35968, 174 interactors |
MINTi | P35968 |
STRINGi | 9606.ENSP00000263923 |
Chemistry databases
BindingDBi | P35968 |
Miscellaneous databases
RNActi | P35968, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P35968 |
BMRBi | P35968 |
SMRi | P35968 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P35968 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 46 – 110 | Ig-like C2-type 1Add BLAST | 65 | |
Domaini | 141 – 207 | Ig-like C2-type 2Add BLAST | 67 | |
Domaini | 224 – 320 | Ig-like C2-type 3Add BLAST | 97 | |
Domaini | 328 – 414 | Ig-like C2-type 4Add BLAST | 87 | |
Domaini | 421 – 548 | Ig-like C2-type 5Add BLAST | 128 | |
Domaini | 551 – 660 | Ig-like C2-type 6Add BLAST | 110 | |
Domaini | 667 – 753 | Ig-like C2-type 7Add BLAST | 87 | |
Domaini | 834 – 1162 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 329 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1274 – 1318 | DisorderedSequence analysisAdd BLAST | 45 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1292 – 1315 | Polar residuesSequence analysisAdd BLAST | 24 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0200, Eukaryota |
GeneTreei | ENSGT00940000156710 |
HOGENOMi | CLU_000288_49_4_1 |
InParanoidi | P35968 |
OMAi | RIFWDSK |
PhylomeDBi | P35968 |
TreeFami | TF325768 |
Family and domain databases
Gene3Di | 2.60.40.10, 7 hits |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR013098, Ig_I-set IPR003599, Ig_sub IPR003598, Ig_sub2 IPR011009, Kinase-like_dom_sf 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 IPR041348, VEGFR-2_TMD IPR009136, VEGFR2_rcpt |
Pfami | View protein in Pfam PF07679, I-set, 2 hits PF07714, PK_Tyr_Ser-Thr, 1 hit PF17988, VEGFR-2_TMD, 1 hit |
PRINTSi | PR01834, VEGFRECEPTR2 |
SMARTi | View protein in SMART SM00409, IG, 7 hits SM00408, IGc2, 5 hits SM00219, TyrKc, 1 hit |
SUPFAMi | SSF48726, SSF48726, 6 hits SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE 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 |
s (3)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2 | Q → E in AAC16450 (Ref. 4) Curated | 1 | |
Sequence conflicti | 772 | A → T in AAA59459 (PubMed:1656371).Curated | 1 | |
Sequence conflicti | 772 | A → T in CAA43837 (PubMed:1656371).Curated | 1 | |
Sequence conflicti | 787 | R → G in AAA59459 (PubMed:1656371).Curated | 1 | |
Sequence conflicti | 787 | R → G in CAA43837 (PubMed:1656371).Curated | 1 | |
Sequence conflicti | 835 | K → N in AAA59459 (PubMed:1656371).Curated | 1 | |
Sequence conflicti | 835 | K → N in CAA43837 (PubMed:1656371).Curated | 1 | |
Sequence conflicti | 1347 | S → T in AAA59459 (PubMed:1656371).Curated | 1 | |
Sequence conflicti | 1347 | S → T in CAA43837 (PubMed:1656371).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_042053 | 2 | Q → R in a lung adenocarcinoma sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_042054 | 136 | V → M1 PublicationCorresponds to variant dbSNP:rs35636987EnsemblClinVar. | 1 | |
Natural variantiVAR_042055 | 248 | A → G in a renal clear cell carcinoma sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_036126 | 275 | R → L in a colorectal cancer sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_022071 | 297 | V → I1 PublicationCorresponds to variant dbSNP:rs2305948EnsemblClinVar. | 1 | |
Natural variantiVAR_042056 | 462 | L → V1 PublicationCorresponds to variant dbSNP:rs56286620EnsemblClinVar. | 1 | |
Natural variantiVAR_020353 | 472 | Q → H2 PublicationsCorresponds to variant dbSNP:rs1870377EnsemblClinVar. | 1 | |
Natural variantiVAR_042057 | 482 | C → R in HCI; associated with disease 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 PublicationsCorresponds to variant dbSNP:rs34231037EnsemblClinVar. | 1 | |
Natural variantiVAR_042058 | 539 | G → R1 PublicationCorresponds to variant dbSNP:rs55716939EnsemblClinVar. | 1 | |
Natural variantiVAR_042059 | 689 | T → M1 PublicationCorresponds to variant dbSNP:rs34038364EnsemblClinVar. | 1 | |
Natural variantiVAR_042060 | 814 | D → N1 PublicationCorresponds to variant dbSNP:rs35603373Ensembl. | 1 | |
Natural variantiVAR_046679 | 848 | V → E Strongly reduced autophosphorylation and kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs1139776Ensembl. | 1 | |
Natural variantiVAR_036127 | 873 | G → R in a colorectal cancer sample; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_046680 | 952 | V → I. Corresponds to variant dbSNP:rs13129474Ensembl. | 1 | |
Natural variantiVAR_042061 | 1065 | A → T1 PublicationCorresponds to variant dbSNP:rs56302315Ensembl. | 1 | |
Natural variantiVAR_063147 | 1147 | P → S in HCI; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121917766EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_041988 | 663 – 678 | ERVAP…ENQTT → GRETILDHCAEAVGMP in isoform 2. 1 PublicationAdd BLAST | 16 | |
Alternative sequenceiVSP_041989 | 679 – 1356 | Missing in isoform 2. 1 PublicationAdd BLAST | 678 | |
Alternative sequenceiVSP_041990 | 712 | G → E in isoform 3. 1 Publication | 1 | |
Alternative sequenceiVSP_041991 | 713 – 1356 | Missing in isoform 3. 1 PublicationAdd BLAST | 644 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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] |
Genome annotation databases
Ensembli | ENST00000263923.5; ENSP00000263923.4; ENSG00000128052.10 |
GeneIDi | 3791 |
KEGGi | hsa:3791 |
MANE-Selecti | ENST00000263923.5; ENSP00000263923.4; NM_002253.4; NP_002244.1 |
UCSCi | uc003has.4, human [P35968-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi 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] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
3WZD | X-ray | 1.57 | A | 814-1172 | [»] | |
3WZE | X-ray | 1.90 | A | 814-1172 | [»] | |
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 | [»] | |
5EW3 | X-ray | 2.50 | A/B | 806-1171 | [»] | |
5OYJ | X-ray | 2.38 | C/D | 326-549 | [»] | |
6GQO | X-ray | 1.87 | A | 806-939 | [»] | |
A | 991-1171 | [»] | ||||
6GQP | X-ray | 2.09 | A | 806-1171 | [»] | |
6GQQ | X-ray | 1.52 | A | 806-939 | [»] | |
A | 991-1171 | [»] | ||||
6XVJ | X-ray | 1.78 | A | 806-1171 | [»] | |
6XVK | X-ray | 1.99 | A | 806-1171 | [»] | |
AlphaFoldDBi | P35968 | |||||
BMRBi | P35968 | |||||
SMRi | P35968 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109992, 77 interactors |
CORUMi | P35968 |
DIPi | DIP-486N |
IntActi | P35968, 174 interactors |
MINTi | P35968 |
STRINGi | 9606.ENSP00000263923 |
Chemistry databases
BindingDBi | P35968 |
ChEMBLi | CHEMBL279 |
DrugBanki | DB04727, 1-{4-[4-Amino-6-(4-methoxyphenyl)furo[2,3-d]pyrimidin-5-yl]phenyl}-3-[2-fluoro-5-(trifluoromethyl)phenyl]urea DB07514, 3-(2-aminoquinazolin-6-yl)-1-(3,3-dimethylindolin-6-yl)-4-methylpyridin-2(1H)-one DB07528, 3-(2-aminoquinazolin-6-yl)-4-methyl-1-[3-(trifluoromethyl)phenyl]pyridin-2(1H)-one DB06938, 4-[[2-[[4-chloro-3-(trifluoromethyl)phenyl]amino]-3H-benzimidazol-5-yl]oxy]-N-methyl-pyridine-2-carboxamide DB07326, 6-chloro-N-pyrimidin-5-yl-3-{[3-(trifluoromethyl)phenyl]amino}-1,2-benzisoxazole-7-carboxamide DB06626, Axitinib DB08875, Cabozantinib DB04849, Cediranib DB05198, CYC116 DB12147, Erdafitinib DB12307, Foretinib DB12010, Fostamatinib DB06101, IMC-1C11 DB09078, Lenvatinib DB06080, Linifanib DB06595, Midostaurin DB07537, N'-(6-aminopyridin-3-yl)-N-(2-cyclopentylethyl)-4-methyl-benzene-1,3-dicarboxamide DB07183, N-(4-phenoxyphenyl)-2-[(pyridin-4-ylmethyl)amino]nicotinamide DB07333, N-(CYCLOPROPYLMETHYL)-4-(METHYLOXY)-3-({5-[3-(3-PYRIDINYL)PHENYL]-1,3-OXAZOL-2-YL}AMINO)BENZENESULFONAMIDE DB07334, N-[5-(ETHYLSULFONYL)-2-METHOXYPHENYL]-5-[3-(2-PYRIDINYL)PHENYL]-1,3-OXAZOL-2-AMINE DB07274, N-cyclopropyl-6-[(6,7-dimethoxyquinolin-4-yl)oxy]naphthalene-1-carboxamide DB09079, Nintedanib DB08519, N~4~-(3-methyl-1H-indazol-6-yl)-N~2~-(3,4,5-trimethoxyphenyl)pyrimidine-2,4-diamine DB08042, N~4~-methyl-N~4~-(3-methyl-1H-indazol-6-yl)-N~2~-(3,4,5-trimethoxyphenyl)pyrimidine-2,4-diamine DB06589, Pazopanib DB05931, Pegdinetanib DB08901, Ponatinib DB15822, Pralsetinib DB05984, RAF-265 DB05578, Ramucirumab DB08896, Regorafenib DB14840, Ripretinib DB06436, Semaxanib DB00398, Sorafenib DB01268, Sunitinib DB05075, TG-100801 DB11800, Tivozanib DB04879, Vatalanib DB05146, XL820 DB05014, XL999 |
DrugCentrali | P35968 |
GuidetoPHARMACOLOGYi | 1813 |
PTM databases
CarbonylDBi | P35968 |
GlyGeni | P35968, 20 sites, 1 O-linked glycan (1 site) |
iPTMneti | P35968 |
PhosphoSitePlusi | P35968 |
Genetic variation databases
BioMutai | KDR |
DMDMi | 9087218 |
Proteomic databases
EPDi | P35968 |
jPOSTi | P35968 |
MassIVEi | P35968 |
MaxQBi | P35968 |
PaxDbi | P35968 |
PeptideAtlasi | P35968 |
PRIDEi | P35968 |
ProteomicsDBi | 55169 [P35968-1] 55170 [P35968-2] 55171 [P35968-3] |
Protocols and materials databases
ABCDi | P35968, 72 sequenced antibodies |
Antibodypediai | 3413, 3852 antibodies from 52 providers |
DNASUi | 3791 |
Genome annotation databases
Ensembli | ENST00000263923.5; ENSP00000263923.4; ENSG00000128052.10 |
GeneIDi | 3791 |
KEGGi | hsa:3791 |
MANE-Selecti | ENST00000263923.5; ENSP00000263923.4; NM_002253.4; NP_002244.1 |
UCSCi | uc003has.4, human [P35968-1] |
Organism-specific databases
CTDi | 3791 |
DisGeNETi | 3791 |
GeneCardsi | KDR |
HGNCi | HGNC:6307, KDR |
HPAi | ENSG00000128052, Low tissue specificity |
MalaCardsi | KDR |
MIMi | 191306, gene 602089, phenotype |
neXtProti | NX_P35968 |
OpenTargetsi | ENSG00000128052 |
Orphaneti | 464293, NON RARE IN EUROPE: Infantile capillary hemangioma 3303, Tetralogy of Fallot |
PharmGKBi | PA30086 |
VEuPathDBi | HostDB:ENSG00000128052 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0200, Eukaryota |
GeneTreei | ENSGT00940000156710 |
HOGENOMi | CLU_000288_49_4_1 |
InParanoidi | P35968 |
OMAi | RIFWDSK |
PhylomeDBi | P35968 |
TreeFami | TF325768 |
Enzyme and pathway databases
BRENDAi | 2.7.10.1, 2681 |
PathwayCommonsi | P35968 |
Reactomei | R-HSA-194306, Neurophilin interactions with VEGF and VEGFR R-HSA-195399, VEGF binds to VEGFR leading to receptor dimerization R-HSA-216083, Integrin cell surface interactions R-HSA-4420097, VEGFA-VEGFR2 Pathway R-HSA-5218921, VEGFR2 mediated cell proliferation R-HSA-9673768, Signaling by membrane-tethered fusions of PDGFRA or PDGFRB |
SignaLinki | P35968 |
SIGNORi | P35968 |
Miscellaneous databases
BioGRID-ORCSi | 3791, 9 hits in 1116 CRISPR screens |
EvolutionaryTracei | P35968 |
GeneWikii | Kinase_insert_domain_receptor |
GenomeRNAii | 3791 |
Pharosi | P35968, Tclin |
PROi | PR:P35968 |
RNActi | P35968, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000128052, Expressed in placenta and 219 other tissues |
ExpressionAtlasi | P35968, baseline and differential |
Genevisiblei | P35968, HS |
Family and domain databases
Gene3Di | 2.60.40.10, 7 hits |
InterProi | View protein in InterPro IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR013098, Ig_I-set IPR003599, Ig_sub IPR003598, Ig_sub2 IPR011009, Kinase-like_dom_sf 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 IPR041348, VEGFR-2_TMD IPR009136, VEGFR2_rcpt |
Pfami | View protein in Pfam PF07679, I-set, 2 hits PF07714, PK_Tyr_Ser-Thr, 1 hit PF17988, VEGFR-2_TMD, 1 hit |
PRINTSi | PR01834, VEGFRECEPTR2 |
SMARTi | View protein in SMART SM00409, IG, 7 hits SM00408, IGc2, 5 hits SM00219, TyrKc, 1 hit |
SUPFAMi | SSF48726, SSF48726, 6 hits SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | VGFR2_HUMAN | |
Accessioni | P35968Primary (citable) accession number: P35968 Secondary accession number(s): A2RRS0 Q14178 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | December 1, 2000 | |
Last modified: | May 25, 2022 | |
This is version 234 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human and mouse protein kinases
Human and mouse protein kinases: classification and index - Human cell differentiation molecules
CD nomenclature of surface proteins of human leucocytes and list of entries - Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families