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Entry version 191 (13 Feb 2019)
Sequence version 1 (01 Jun 1994)
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Protein

Vascular endothelial growth factor receptor 2

Gene

Kdr

Organism
Mus musculus (Mouse)
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, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as a negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and by 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.8 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. May be regulated by hydrogen sulfide (H2S) levels via a sensitive intracellular disulfide bond (By similarity).By similarity

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 sitei866ATPPROSITE-ProRule annotation1
<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 sitei1026Proton 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 bindingi838 – 846ATPPROSITE-ProRule annotation9

<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
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 3474

<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 NYK
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:Flk-1, Flk1
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:96683 Kdr

<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 – 762ExtracellularSequence analysisAdd BLAST743
<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>Transmembranei763 – 783HelicalSequence analysisAdd BLAST21
Topological domaini784 – 1367CytoplasmicSequence analysisAdd BLAST584

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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic lethality at 8.5 to 9.5 dpc, due to early defects in the development of hematopoietic and endothelial cells, leading to defects in vasculogenesis and endocardium development. At 7.5 dpc, there are no blood islands in the yolk sac. Organized blood vessels are absent in the yolk sac and in the embryo.1 Publication

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>Mutagenesisi866K → R: Loss of enzyme activity. Abolishes ubiquitination in response to VEGFA binding. 1 Publication1
Mutagenesisi1173Y → F: Loss of interaction with SHB. 1 Publication1
Mutagenesisi1188S → A: Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1191. 1 Publication1
Mutagenesisi1191S → A: Strongly reduces internalization and down-regulation of the activated receptor; when associated with A-1188. 1 Publication1
Mutagenesisi1212Y → F: Strongly reduced autophosphorylation. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3337

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1813

<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_000001677220 – 1367Vascular endothelial growth factor receptor 2Add BLAST1348

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 ↔ 105PROSITE-ProRule annotation
Glycosylationi98N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi145N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi152 ↔ 202PROSITE-ProRule annotation
Glycosylationi160N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi247N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi248 ↔ 309PROSITE-ProRule annotation
Glycosylationi320N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi376N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi397N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi447 ↔ 528PROSITE-ProRule annotation
Glycosylationi509N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi521N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi569 ↔ 640PROSITE-ProRule annotation
Glycosylationi578N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi611N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi617N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi629N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi673N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi686 ↔ 735PROSITE-ProRule annotation
Glycosylationi702N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi719N-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 residuei799PhosphotyrosineBy similarity1
Modified residuei949Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei980PhosphoserineBy similarity1
Modified residuei982PhosphoserineBy similarity1
Modified residuei994Phosphotyrosine; by autocatalysisBy similarity1
Disulfide bondi1022 ↔ 1043Redox-activePROSITE-ProRule annotation
Modified residuei1052Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1057Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1173Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1212Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1229PhosphoserineCombined sources1
Modified residuei1233PhosphoserineCombined sources1
Modified residuei1236PhosphothreonineCombined sources1
Modified residuei1303Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1307Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1317Phosphotyrosine; by autocatalysisBy similarity1

<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.By similarity
Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases (By similarity).By similarity
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-949 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1173 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1212 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRJ at Tyr-799, Tyr-949, Tyr-994, Tyr-1052, Tyr-1057, Tyr-1173 and Tyr-1212 (By similarity).By similarity
The inhibitory disulfide bond between Cys-1022 and Cys-1043 may serve as a specific molecular switch for H2S-induced modification that regulates VEGFR2 function.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P35918

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

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PaxDbi
P35918

PRoteomics IDEntifications database

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PRIDEi
P35918

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35918

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

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PhosphoSitePlusi
P35918

<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

Expressed in endothelial cells (at protein level). Detected in embryonic endothelial cells, as well as hematopoietic stem and progenitor cells. Detected in vascular endothelium. Expressed at high levels in adult heart, lung, kidney, brain and skeletal muscle, but is also expressed at lower levels in most other adult tissues.4 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in endothelial cells of allantois/umbilical vessels at 8.5 dpc (at protein level). Increases moderately during pregnancy (maximum 2.7-fold at 19 days), and increases further during lactation (maximum 3.7-fold increase on day 7).2 Publications

<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 (PubMed:12796773, PubMed:12881528, PubMed:15026417, PubMed:15673613, PubMed:17702744, PubMed:19668192, PubMed:7681362, PubMed:8356051). 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 (By similarity).By similarity8 Publications

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>Sitei1173Interaction with SHB1

<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

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P35918

Database of interacting proteins

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DIPi
DIP-215N

Protein interaction database and analysis system

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IntActi
P35918, 13 interactors

Molecular INTeraction database

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MINTi
P35918

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000109144

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35918

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P35918

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

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SMRi
P35918

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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 – 111Ig-like C2-type 1Add BLAST66
Domaini143 – 209Ig-like C2-type 2Add BLAST67
Domaini226 – 325Ig-like C2-type 3Add BLAST100
Domaini330 – 416Ig-like C2-type 4Add BLAST87
Domaini423 – 542Ig-like C2-type 5Add BLAST120
Domaini549 – 656Ig-like C2-type 6Add BLAST108
Domaini665 – 751Ig-like C2-type 7Add BLAST87
Domaini832 – 1160Protein 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.By similarity

<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

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eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000037949

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053432

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35918

Database for complete collections of gene phylogenies

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PhylomeDBi
P35918

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 7 hits

Integrated resource of protein families, domains and functional sites

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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
IPR009136 VEGFR2_rcpt

The PANTHER Classification System

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PANTHERi
PTHR24416:SF45 PTHR24416:SF45, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01834 VEGFRECEPTR2

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 4 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48726 SSF48726, 7 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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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 (2+)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 2 <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

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P35918-1) [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
MESKALLAVA LWFCVETRAA SVGLPGDFLH PPKLSTQKDI LTILANTTLQ
60 70 80 90 100
ITCRGQRDLD WLWPNAQRDS EERVLVTECG GGDSIFCKTL TIPRVVGNDT
110 120 130 140 150
GAYKCSYRDV DIASTVYVYV RDYRSPFIAS VSDQHGIVYI TENKNKTVVI
160 170 180 190 200
PCRGSISNLN VSLCARYPEK RFVPDGNRIS WDSEIGFTLP SYMISYAGMV
210 220 230 240 250
FCEAKINDET YQSIMYIVVV VGYRIYDVIL SPPHEIELSA GEKLVLNCTA
260 270 280 290 300
RTELNVGLDF TWHSPPSKSH HKKIVNRDVK PFPGTVAKMF LSTLTIESVT
310 320 330 340 350
KSDQGEYTCV ASSGRMIKRN RTFVRVHTKP FIAFGSGMKS LVEATVGSQV
360 370 380 390 400
RIPVKYLSYP APDIKWYRNG RPIESNYTMI VGDELTIMEV TERDAGNYTV
410 420 430 440 450
ILTNPISMEK QSHMVSLVVN VPPQIGEKAL ISPMDSYQYG TMQTLTCTVY
460 470 480 490 500
ANPPLHHIQW YWQLEEACSY RPGQTSPYAC KEWRHVEDFQ GGNKIEVTKN
510 520 530 540 550
QYALIEGKNK TVSTLVIQAA NVSALYKCEA INKAGRGERV ISFHVIRGPE
560 570 580 590 600
ITVQPAAQPT EQESVSLLCT ADRNTFENLT WYKLGSQATS VHMGESLTPV
610 620 630 640 650
CKNLDALWKL NGTMFSNSTN DILIVAFQNA SLQDQGDYVC SAQDKKTKKR
660 670 680 690 700
HCLVKQLIIL ERMAPMITGN LENQTTTIGE TIEVTCPASG NPTPHITWFK
710 720 730 740 750
DNETLVEDSG IVLRDGNRNL TIRRVRKEDG GLYTCQACNV LGCARAETLF
760 770 780 790 800
IIEGAQEKTN LEVIILVGTA VIAMFFWLLL VILVRTVKRA NEGELKTGYL
810 820 830 840 850
SIVMDPDELP LDERCERLPY DASKWEFPRD RLKLGKPLGR GAFGQVIEAD
860 870 880 890 900
AFGIDKTATC KTVAVKMLKE GATHSEHRAL MSELKILIHI GHHLNVVNLL
910 920 930 940 950
GACTKPGGPL MVIVEFSKFG NLSTYLRGKR NEFVPYKSKG ARFRQGKDYV
960 970 980 990 1000
GELSVDLKRR LDSITSSQSS ASSGFVEEKS LSDVEEEEAS EELYKDFLTL
1010 1020 1030 1040 1050
EHLICYSFQV AKGMEFLASR KCIHRDLAAR NILLSEKNVV KICDFGLARD
1060 1070 1080 1090 1100
IYKDPDYVRK GDARLPLKWM APETIFDRVY TIQSDVWSFG VLLWEIFSLG
1110 1120 1130 1140 1150
ASPYPGVKID EEFCRRLKEG TRMRAPDYTT PEMYQTMLDC WHEDPNQRPS
1160 1170 1180 1190 1200
FSELVEHLGN LLQANAQQDG KDYIVLPMSE TLSMEEDSGL SLPTSPVSCM
1210 1220 1230 1240 1250
EEEEVCDPKF HYDNTAGISH YLQNSKRKSR PVSVKTFEDI PLEEPEVKVI
1260 1270 1280 1290 1300
PDDSQTDSGM VLASEELKTL EDRNKLSPSF GGMMPSKSRE SVASEGSNQT
1310 1320 1330 1340 1350
SGYQSGYHSD DTDTTVYSSD EAGLLKMVDA AVHADSGTTL QLTSCLNGSG
1360
PVPAPPPTPG NHERGAA
Length:1,367
Mass (Da):152,517
Last modified:June 1, 1994 - v1
<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:iEFC99704F1DCA266
GO
Isoform 2 (identifier: P35918-2) [UniParc]FASTAAdd to basket
Also known as: sVegfr-2

The sequence of this isoform differs from the canonical sequence as follows:
     661-673: ERMAPMITGNLEN → GMEASLGDRIAMP
     674-1367: Missing.

Show »
Length:673
Mass (Da):75,230
Checksum:iCCEFE9DA9B53B300
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q8VCD0Q8VCD0_MOUSE
Kinase insert domain protein recept...
Kdr mCG_7209
1,345Annotation score:

Annotation score:4 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 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 conflicti25P → T in CAA50192 (PubMed:7681362).Curated1
Sequence conflicti679G → D in AAB25043 (PubMed:8423988).Curated1
Sequence conflicti783 – 784LV → VL in CAA50192 (PubMed:7681362).Curated2
Sequence conflicti917S → C in CAA50192 (PubMed:7681362).Curated1
Sequence conflicti1341 – 1367QLTSC…ERGAA → RSPPV in AAB25043 (PubMed:8423988).CuratedAdd BLAST27

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_041986661 – 673ERMAP…GNLEN → GMEASLGDRIAMP in isoform 2. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_041987674 – 1367Missing in isoform 2. 1 PublicationAdd BLAST694

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
X70842 mRNA Translation: CAA50192.1
X59397 mRNA Translation: CAA42040.1
S53103 mRNA Translation: AAB25043.1
EU884114 mRNA Translation: ACJ66293.1
X89777 Genomic DNA Translation: CAA61917.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A41228

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.285

Genome annotation databases

UCSC genome browser

More...
UCSCi
uc012dxk.2 mouse [P35918-2]

Keywords - Coding sequence diversityi

Alternative splicing

<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
X70842 mRNA Translation: CAA50192.1
X59397 mRNA Translation: CAA42040.1
S53103 mRNA Translation: AAB25043.1
EU884114 mRNA Translation: ACJ66293.1
X89777 Genomic DNA Translation: CAA61917.1
PIRiA41228
UniGeneiMm.285

3D structure databases

ProteinModelPortaliP35918
SMRiP35918
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

CORUMiP35918
DIPiDIP-215N
IntActiP35918, 13 interactors
MINTiP35918
STRINGi10090.ENSMUSP00000109144

Chemistry databases

BindingDBiP35918
ChEMBLiCHEMBL3337
GuidetoPHARMACOLOGYi1813

PTM databases

iPTMnetiP35918
PhosphoSitePlusiP35918

Proteomic databases

MaxQBiP35918
PaxDbiP35918
PRIDEiP35918

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc012dxk.2 mouse [P35918-2]

Organism-specific databases

MGIiMGI:96683 Kdr

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
HOGENOMiHOG000037949
HOVERGENiHBG053432
InParanoidiP35918
PhylomeDBiP35918

Enzyme and pathway databases

BRENDAi2.7.10.1 3474

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Kdr mouse

Protein Ontology

More...
PROi
PR:P35918

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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
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
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR01834 VEGFRECEPTR2
SMARTiView protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 4 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 7 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

More...
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_MOUSE
<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: P35918
Secondary accession number(s): C5H7S5
<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: June 1, 1994
Last modified: February 13, 2019
This is version 191 of the entry and version 1 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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