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Entry version 215 (13 Feb 2019)
Sequence version 2 (01 Dec 2000)
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Protein

Vascular endothelial growth factor receptor 2

Gene

KDR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei868ATPCurated1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1028Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi840 – 848ATPCurated9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processAngiogenesis, Differentiation, Host-virus interaction
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P35968

SIGNOR Signaling Network Open Resource

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SIGNORi
P35968

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:KDR
Synonyms:FLK1, VEGFR2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000128052.8

Human Gene Nomenclature Database

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HGNCi
HGNC:6307 KDR

Online Mendelian Inheritance in Man (OMIM)

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MIMi
191306 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P35968

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini20 – 764ExtracellularSequence analysisAdd BLAST745
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei765 – 785HelicalSequence analysisAdd BLAST21
Topological domaini786 – 1356CytoplasmicSequence analysisAdd BLAST571

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hemangioma, capillary infantile (HCI)3 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:602089
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_042057482C → 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_0631471147P → S in HCI; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121917766EnsemblClinVar.1
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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi726R → A: Strongly reduced autophosphorylation and activation of MAP kinases. 1 Publication1
Mutagenesisi731D → A: Strongly reduced autophosphorylation and activation of MAP kinases. 1 Publication1
Mutagenesisi801Y → F: Abolishes stimulation of nitric oxide synthesis. 1 Publication1
Mutagenesisi868K → M: Loss of enzyme activity. 1 Publication1
Mutagenesisi951Y → F: Abolishes reorganization of the actin cytoskeleton and cell migration in response to VEGFA. 1 Publication1
Mutagenesisi996Y → F: Strongly reduced autophosphorylation. Reduces phosphorylation of PLCG1. 1 Publication1
Mutagenesisi1045C → A: Significantly higher kinase activity. 1 Publication1
Mutagenesisi1054Y → F: Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1059. 1 Publication1
Mutagenesisi1059Y → F: Strongly reduced autophosphorylation. Abolishes phosphorylation of downstream signaling proteins; when associated with F-1054. 1 Publication1
Mutagenesisi1175Y → F: Abolishes phosphorylation of PLCG1 and MAP kinases in response to VEGFA. 1 Publication1
Mutagenesisi1214Y → F: Loss of phosphorylation site. Abolishes reorganization of the actin cytoskeleton in response to VEGFA. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
3791

MalaCards human disease database

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MalaCardsi
KDR
MIMi602089 phenotype

Open Targets

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OpenTargetsi
ENSG00000128052

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
464293 NON RARE IN EUROPE: Infantile capillary hemangioma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30086

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL279

Drug and drug target database

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DrugBanki
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
DB06080 ABT-869
DB06626 Axitinib
DB04849 AZD2171
DB08875 Cabozantinib
DB05198 CYC116
DB06101 IMC-1C11
DB09078 Lenvatinib
DB07183 N-(4-phenoxyphenyl)-2-[(pyridin-4-ylmethyl)amino]nicotinamide
DB09079 Nintedanib
DB06589 Pazopanib
DB08901 Ponatinib
DB05578 Ramucirumab
DB08896 Regorafenib
DB00398 Sorafenib
DB01268 Sunitinib
DB05075 TG100801
DB04879 Vatalanib
DB05153 XL184
DB05146 XL820
DB05030 XL880
DB05014 XL999

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1813

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
KDR

Domain mapping of disease mutations (DMDM)

More...
DMDMi
9087218

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Sequence analysisAdd BLAST19
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001677120 – 1356Vascular endothelial growth factor receptor 2Add BLAST1337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi46N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi53 ↔ 103PROSITE-ProRule annotation
Glycosylationi66N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi96N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi143N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi150 ↔ 200
Glycosylationi158N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi245N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi246 ↔ 307
Glycosylationi318N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi374N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi395N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi445 ↔ 530PROSITE-ProRule annotation
Glycosylationi511N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi523N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi571 ↔ 642PROSITE-ProRule annotation
Glycosylationi580N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi613N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi619N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi631N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi675N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi688 ↔ 737PROSITE-ProRule annotation
Glycosylationi704N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi721N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei801Phosphotyrosine2 Publications1
Modified residuei951Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei982PhosphoserineCombined sources1
Modified residuei984PhosphoserineCombined sources1
Modified residuei996Phosphotyrosine; by autocatalysis2 Publications1
Disulfide bondi1024 ↔ 1045Redox-active
Modified residuei1054Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei1059Phosphotyrosine; by autocatalysis6 Publications1
Modified residuei1175Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei1214Phosphotyrosine; by autocatalysis4 Publications1
Modified residuei1231PhosphoserineBy similarity1
Modified residuei1235PhosphoserineBy similarity1
Modified residuei1238PhosphothreonineBy similarity1
Modified residuei1305Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1309Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1319Phosphotyrosine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P35968

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P35968

MaxQB - The MaxQuant DataBase

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MaxQBi
P35968

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P35968

PeptideAtlas

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PeptideAtlasi
P35968

PRoteomics IDEntifications database

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PRIDEi
P35968

ProteomicsDB human proteome resource

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ProteomicsDBi
55169
55170 [P35968-2]
55171 [P35968-3]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P35968

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35968

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P35968

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000128052 Expressed in 208 organ(s), highest expression level in lung

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P35968 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35968 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004028

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (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).22 Publications
(Microbial infection) Interacts with HIV-1 Tat.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1175Interaction with SHBBy similarity1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109992, 60 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P35968

Database of interacting proteins

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DIPi
DIP-486N

Protein interaction database and analysis system

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IntActi
P35968, 41 interactors

Molecular INTeraction database

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MINTi
P35968

STRING: functional protein association networks

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STRINGi
9606.ENSP00000263923

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35968

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
3WZDX-ray1.57A814-1172[»]
3WZEX-ray1.90A814-1172[»]
4AG8X-ray1.95A806-1171[»]
4AGCX-ray2.00A787-1171[»]
4AGDX-ray2.81A787-1171[»]
4ASDX-ray2.03A787-1171[»]
4ASEX-ray1.83A787-1171[»]
5EW3X-ray2.50A/B806-1171[»]
5OYJX-ray2.38C/D326-549[»]
6GQOX-ray1.87A806-939[»]
A991-1171[»]
6GQPX-ray2.09A806-1171[»]
6GQQX-ray1.52A806-939[»]
A991-1171[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P35968

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P35968

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P35968

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini46 – 110Ig-like C2-type 1Add BLAST65
Domaini141 – 207Ig-like C2-type 2Add BLAST67
Domaini224 – 320Ig-like C2-type 3Add BLAST97
Domaini328 – 414Ig-like C2-type 4Add BLAST87
Domaini421 – 548Ig-like C2-type 5Add BLAST128
Domaini551 – 660Ig-like C2-type 6Add BLAST110
Domaini667 – 753Ig-like C2-type 7Add BLAST87
Domaini834 – 1162Protein kinasePROSITE-ProRule annotationAdd BLAST329

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156710

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG053432

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P35968

KEGG Orthology (KO)

More...
KOi
K05098

Identification of Orthologs from Complete Genome Data

More...
OMAi
TIMANTT

Database of Orthologous Groups

More...
OrthoDBi
384993at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P35968

TreeFam database of animal gene trees

More...
TreeFami
TF325768

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 7 hits

Integrated resource of protein families, domains and functional sites

More...
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
IPR013151 Immunoglobulin
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
IPR009136 VEGFR2_rcpt

The PANTHER Classification System

More...
PANTHERi
PTHR24416:SF45 PTHR24416:SF45, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07679 I-set, 2 hits
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01834 VEGFRECEPTR2

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 5 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 6 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2Q → E in AAC16450 (Ref. 4) Curated1
Sequence conflicti772A → T in AAA59459 (PubMed:1656371).Curated1
Sequence conflicti772A → T in CAA43837 (PubMed:1656371).Curated1
Sequence conflicti787R → G in AAA59459 (PubMed:1656371).Curated1
Sequence conflicti787R → G in CAA43837 (PubMed:1656371).Curated1
Sequence conflicti835K → N in AAA59459 (PubMed:1656371).Curated1
Sequence conflicti835K → N in CAA43837 (PubMed:1656371).Curated1
Sequence conflicti1347S → T in AAA59459 (PubMed:1656371).Curated1
Sequence conflicti1347S → T in CAA43837 (PubMed:1656371).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0420532Q → R in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042054136V → M1 PublicationCorresponds to variant dbSNP:rs35636987EnsemblClinVar.1
Natural variantiVAR_042055248A → G in a renal clear cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_036126275R → L in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_022071297V → I1 PublicationCorresponds to variant dbSNP:rs2305948EnsemblClinVar.1
Natural variantiVAR_042056462L → V1 PublicationCorresponds to variant dbSNP:rs56286620EnsemblClinVar.1
Natural variantiVAR_020353472Q → H2 PublicationsCorresponds to variant dbSNP:rs1870377EnsemblClinVar.1
Natural variantiVAR_042057482C → 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_042058539G → R1 PublicationCorresponds to variant dbSNP:rs55716939EnsemblClinVar.1
Natural variantiVAR_042059689T → M1 PublicationCorresponds to variant dbSNP:rs34038364EnsemblClinVar.1
Natural variantiVAR_042060814D → N1 PublicationCorresponds to variant dbSNP:rs35603373Ensembl.1
Natural variantiVAR_046679848V → E Strongly reduced autophosphorylation and kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs1139776Ensembl.1
Natural variantiVAR_036127873G → R in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_046680952V → I. Corresponds to variant dbSNP:rs13129474Ensembl.1
Natural variantiVAR_0420611065A → T1 PublicationCorresponds to variant dbSNP:rs56302315Ensembl.1
Natural variantiVAR_0631471147P → S in HCI; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121917766EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041988663 – 678ERVAP…ENQTT → GRETILDHCAEAVGMP in isoform 2. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_041989679 – 1356Missing in isoform 2. 1 PublicationAdd BLAST678
Alternative sequenceiVSP_041990712G → E in isoform 3. 1 Publication1
Alternative sequenceiVSP_041991713 – 1356Missing in isoform 3. 1 PublicationAdd BLAST644

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3497.1 [P35968-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC1402

NCBI Reference Sequences

More...
RefSeqi
NP_002244.1, NM_002253.2 [P35968-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.479756

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000263923; ENSP00000263923; ENSG00000128052 [P35968-1]
ENST00000645273; ENSP00000495159; ENSG00000128052 [P35968-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3791

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3791

UCSC genome browser

More...
UCSCi
uc003has.4 human [P35968-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
CCDSiCCDS3497.1 [P35968-1]
PIRiJC1402
RefSeqiNP_002244.1, NM_002253.2 [P35968-1]
UniGeneiHs.479756

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
3WZDX-ray1.57A814-1172[»]
3WZEX-ray1.90A814-1172[»]
4AG8X-ray1.95A806-1171[»]
4AGCX-ray2.00A787-1171[»]
4AGDX-ray2.81A787-1171[»]
4ASDX-ray2.03A787-1171[»]
4ASEX-ray1.83A787-1171[»]
5EW3X-ray2.50A/B806-1171[»]
5OYJX-ray2.38C/D326-549[»]
6GQOX-ray1.87A806-939[»]
A991-1171[»]
6GQPX-ray2.09A806-1171[»]
6GQQX-ray1.52A806-939[»]
A991-1171[»]
ProteinModelPortaliP35968
SMRiP35968
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109992, 60 interactors
CORUMiP35968
DIPiDIP-486N
IntActiP35968, 41 interactors
MINTiP35968
STRINGi9606.ENSP00000263923

Chemistry databases

BindingDBiP35968
ChEMBLiCHEMBL279
DrugBankiDB07528 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
DB06080 ABT-869
DB06626 Axitinib
DB04849 AZD2171
DB08875 Cabozantinib
DB05198 CYC116
DB06101 IMC-1C11
DB09078 Lenvatinib
DB07183 N-(4-phenoxyphenyl)-2-[(pyridin-4-ylmethyl)amino]nicotinamide
DB09079 Nintedanib
DB06589 Pazopanib
DB08901 Ponatinib
DB05578 Ramucirumab
DB08896 Regorafenib
DB00398 Sorafenib
DB01268 Sunitinib
DB05075 TG100801
DB04879 Vatalanib
DB05153 XL184
DB05146 XL820
DB05030 XL880
DB05014 XL999
GuidetoPHARMACOLOGYi1813

PTM databases

CarbonylDBiP35968
iPTMnetiP35968
PhosphoSitePlusiP35968

Polymorphism and mutation databases

BioMutaiKDR
DMDMi9087218

Proteomic databases

EPDiP35968
jPOSTiP35968
MaxQBiP35968
PaxDbiP35968
PeptideAtlasiP35968
PRIDEiP35968
ProteomicsDBi55169
55170 [P35968-2]
55171 [P35968-3]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
3791
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263923; ENSP00000263923; ENSG00000128052 [P35968-1]
ENST00000645273; ENSP00000495159; ENSG00000128052 [P35968-1]
GeneIDi3791
KEGGihsa:3791
UCSCiuc003has.4 human [P35968-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3791
DisGeNETi3791
EuPathDBiHostDB:ENSG00000128052.8

GeneCards: human genes, protein and diseases

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GeneCardsi
KDR
HGNCiHGNC:6307 KDR
HPAiCAB004028
MalaCardsiKDR
MIMi191306 gene
602089 phenotype
neXtProtiNX_P35968
OpenTargetsiENSG00000128052
Orphaneti464293 NON RARE IN EUROPE: Infantile capillary hemangioma
PharmGKBiPA30086

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000156710
HOVERGENiHBG053432
InParanoidiP35968
KOiK05098
OMAiTIMANTT
OrthoDBi384993at2759
PhylomeDBiP35968
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-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
SignaLinkiP35968
SIGNORiP35968

Miscellaneous databases

EvolutionaryTraceiP35968

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Kinase_insert_domain_receptor

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
3791

Protein Ontology

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PROi
PR:P35968

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000128052 Expressed in 208 organ(s), highest expression level in lung
ExpressionAtlasiP35968 baseline and differential
GenevisibleiP35968 HS

Family and domain databases

Gene3Di2.60.40.10, 7 hits
InterProiView 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
IPR013151 Immunoglobulin
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
IPR009136 VEGFR2_rcpt
PANTHERiPTHR24416:SF45 PTHR24416:SF45, 1 hit
PfamiView protein in Pfam
PF07679 I-set, 2 hits
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR01834 VEGFRECEPTR2
SMARTiView protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 5 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 6 hits
SSF56112 SSF56112, 1 hit
PROSITEiView 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVGFR2_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P35968
Secondary accession number(s): A2RRS0
, B5A925, C5IFA0, O60723, Q14178
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: February 13, 2019
This is version 215 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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