Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 165 (08 May 2019)
Sequence version 1 (01 Jul 1997)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Vascular endothelial growth factor receptor 2

Gene

Kdr

Organism
Rattus norvegicus (Rat)
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 may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. 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 (By similarity).By similarity

<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 sitei864ATPPROSITE-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 sitei1024Proton 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 bindingi836 – 844ATPPROSITE-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 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-194306 Neurophilin interactions with VEGF and VEGFR
R-RNO-195399 VEGF binds to VEGFR leading to receptor dimerization
R-RNO-216083 Integrin cell surface interactions
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-5218921 VEGFR2 mediated cell proliferation

<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
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
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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

Rat genome database

More...
RGDi
2965 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 – 760ExtracellularSequence analysisAdd BLAST741
<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>Transmembranei761 – 781HelicalSequence analysisAdd BLAST21
Topological domaini782 – 1343CytoplasmicSequence analysisAdd BLAST562

Keywords - Cellular componenti

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

<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_000001677320 – 1343Vascular endothelial growth factor receptor 2Add BLAST1324

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
Glycosylationi96N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi143N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi150 ↔ 200PROSITE-ProRule annotation
Glycosylationi158N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi245N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi246 ↔ 307PROSITE-ProRule annotation
Glycosylationi318N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi374N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi395N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi445 ↔ 526PROSITE-ProRule annotation
Glycosylationi507N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi567 ↔ 638PROSITE-ProRule annotation
Glycosylationi576N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi609N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi615N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi627N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi671N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi684 ↔ 733PROSITE-ProRule annotation
Glycosylationi700N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi717N-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 residuei797PhosphotyrosineBy similarity1
Modified residuei947Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei978PhosphoserineCombined sources1
Modified residuei980PhosphoserineCombined sources1
Modified residuei992Phosphotyrosine; by autocatalysisBy similarity1
Disulfide bondi1020 ↔ 1041Redox-activePROSITE-ProRule annotation
Modified residuei1050Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1055Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1171Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1210Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1227PhosphoserineBy similarity1
Modified residuei1231PhosphoserineBy similarity1
Modified residuei1234PhosphothreonineBy similarity1
Modified residuei1301Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1305Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1315Phosphotyrosine; 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-947 is important for interaction with SH2D2A/TSAD and VEGFA-mediated reorganization of the actin cytoskeleton. Phosphorylation at Tyr-1171 is important for interaction with PLCG1 and SHB. Phosphorylation at Tyr-1210 is important for interaction with NCK1 and FYN. Dephosphorylated by PTPRB. Dephosphorylated by PTPRJ at Tyr-797, Tyr-947, Tyr-992, Tyr-1050, Tyr-1055, Tyr-1171 and Tyr-1210 (By similarity).By similarity
The inhibitory disulfide bond between Cys-1020 and Cys-1041 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

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O08775

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

More...
PaxDbi
O08775

PRoteomics IDEntifications database

More...
PRIDEi
O08775

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O08775

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

More...
PhosphoSitePlusi
O08775

<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 the post-pubertal mammary glands.1 Publication

<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

Increases during pregnancy (1.6-fold at 4 days) and lactation (3.8-fold at 7 days). Decreases in the early phases of involution (45%, 50% and 34% on days 1, 2, and 3 respectively).1 Publication

<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- and vascular endothelial growth factor (VEGF)-dependent manner in endothelial cells (By similarity).By similarity

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>Sitei1171Interaction with SHBBy similarity1

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
O08775, 1 interactor

Molecular INTeraction database

More...
MINTi
O08775

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000066886

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O08775

<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

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

More...
SMRi
O08775

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 – 109Ig-like C2-type 1Add BLAST64
Domaini141 – 207Ig-like C2-type 2Add BLAST67
Domaini224 – 320Ig-like C2-type 3Add BLAST97
Domaini328 – 414Ig-like C2-type 4Add BLAST87
Domaini421 – 540Ig-like C2-type 5Add BLAST120
Domaini547 – 654Ig-like C2-type 6Add BLAST108
Domaini663 – 749Ig-like C2-type 7Add BLAST87
Domaini830 – 1158Protein 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

More...
eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O08775

KEGG Orthology (KO)

More...
KOi
K05098

Database of Orthologous Groups

More...
OrthoDBi
236292at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O08775

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
IPR041348 VEGFR-2_TMD
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
PF17988 VEGFR-2_TMD, 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, 7 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

O08775-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MESRALLAVA LWFCVETRAA SVGLPGDSLH PPKLSTQKDI LTILANTTLQ
60 70 80 90 100
ITCRGQRDLD WLWPNTPRDS EERVLVTECG DSIFCKTLTV PRVVGNDTGA
110 120 130 140 150
YKCFYRDTDV SSIVYVYVQD HRSPFIASVS DEHGIVYITE NKNKTVVIPC
160 170 180 190 200
RGSISNLNVS LCARYPEKRF VPDGNRISWD SEKGFTIPSY MISYAGMVFC
210 220 230 240 250
EAKINDETYQ SIMYIVLVVG YRIYDVVLSP PHEIELSAGE KLVLNCTART
260 270 280 290 300
ELNVGLDFSW QFPSSKHQHK KIVNRDVKSL PGTVAKMFLS TLTIDSVTKS
310 320 330 340 350
DQGEYTCTAY SGLMTKKNKT FVRVHTKPFI AFGSGMKSLV EATVGSQVRI
360 370 380 390 400
PVKYLSYPAP DIKWYRNGRP IESNYTMIVG DELTIMEVSE RDAGNYTVIL
410 420 430 440 450
TNPISMEKQS HMVSLVVNVP PQIGEKALIS PMDSYQYGTM QTLTCTVYAN
460 470 480 490 500
PPLHHIQWYW QLEEACSYRP SQTNPYTCKE WRHVKDFQGG NKIEVTKNQY
510 520 530 540 550
ALIEGKNKTV STLVIQAAYV SALYKCEAIN KAGRGERVIS FHVIRGPEIT
560 570 580 590 600
VQPATQPTER ESMSLLCTAD RNTFENLTWY KLGSQATSVH MGESLTPVCK
610 620 630 640 650
NLDALWKLNG TVFSNSTNDI LIVAFQNASL QDQGNYVCSA QDKKTKKRHC
660 670 680 690 700
LVKQLVILER MAPMITGNLE NQTTTIGETI EVVCPTSGNP TPLITWFKDN
710 720 730 740 750
ETLVEDSGIV LKDGNRNLTI RRVRKEDGGL YTCQACNVLG CARAETLFII
760 770 780 790 800
EGVQEKTNLE VIILVGTAVI AMFFWLLLVI LVRTVKRANE GELKTGYLSI
810 820 830 840 850
VMDPDELPLD ERCERLPYDA SKWEFPRDRL KLGKPLGRGA FGQVIEADAF
860 870 880 890 900
GIDKTATCKT VAVKMLKEGA THSEHRALMS ELKILIHIGH HLNVVNLLGA
910 920 930 940 950
CTKPGGPLMV IVEFCKFGNL STYLRGKRNE FVPYKSKGAR FRSGKDYVGE
960 970 980 990 1000
LSVDLKRRLD SITSSQSSAS SGFVEEKSLS DVEEEEASEE LYKDFLTLEH
1010 1020 1030 1040 1050
LICYSFQVAK GMEFLASRKC IHRDLAARNI LLSEKNVVKI CDFGLARDIY
1060 1070 1080 1090 1100
KDPDYVRKGD PRLPLKWMAP ETIFDRIYTI QSGVWSFGVL LWEIFSLGAS
1110 1120 1130 1140 1150
PYPGVKIDEK FCRRLKEGTR MRAPDYTTPE MYQTMLDCWH EDPNQRPAFS
1160 1170 1180 1190 1200
ELVEHLGNLL QANAQQDGKD YIVLPMSETL SMEEDSGLSL PTSPVSCMEE
1210 1220 1230 1240 1250
EEVCDPKFHY DNTAGISHYL QNSKRKSRPV SVKTFEDIPL EEPEVKVIPD
1260 1270 1280 1290 1300
DSQTDSGMVL ASEELKTLED RNKLSPSFGG MMPSKSRESV ASEGSNQTSG
1310 1320 1330 1340
YQSGYHSDDT DTTVYSSDEA GLLKLVDVAG HVDSGTTLRS SPV
Length:1,343
Mass (Da):150,394
Last modified:July 1, 1997 - 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:iAD7E509EB62D3FF4
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5PQU0Q5PQU0_RAT
Kdr protein
Kdr rCG_56984
1,343Annotation 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>
A0A0G2JW10A0A0G2JW10_RAT
Receptor protein-tyrosine kinase
Kdr
991Annotation score:

Annotation score:2 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U93306 mRNA Translation: AAB97508.1
U93307 mRNA Translation: AAB97509.1

NCBI Reference Sequences

More...
RefSeqi
NP_037194.1, NM_013062.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25589

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25589

<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
U93306 mRNA Translation: AAB97508.1
U93307 mRNA Translation: AAB97509.1
RefSeqiNP_037194.1, NM_013062.1

3D structure databases

SMRiO08775
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08775, 1 interactor
MINTiO08775
STRINGi10116.ENSRNOP00000066886

Chemistry databases

BindingDBiO08775

PTM databases

iPTMnetiO08775
PhosphoSitePlusiO08775

Proteomic databases

jPOSTiO08775
PaxDbiO08775
PRIDEiO08775

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25589
KEGGirno:25589

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3791
RGDi2965 Kdr

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
InParanoidiO08775
KOiK05098
OrthoDBi236292at2759
PhylomeDBiO08775

Enzyme and pathway databases

BRENDAi2.7.10.1 5301
ReactomeiR-RNO-194306 Neurophilin interactions with VEGF and VEGFR
R-RNO-195399 VEGF binds to VEGFR leading to receptor dimerization
R-RNO-216083 Integrin cell surface interactions
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-5218921 VEGFR2 mediated cell proliferation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O08775

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
IPR041348 VEGFR-2_TMD
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
PF17988 VEGFR-2_TMD, 1 hit
PRINTSiPR01834 VEGFRECEPTR2
SMARTiView protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 5 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_RAT
<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: O08775
<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: December 1, 2000
Last sequence update: July 1, 1997
Last modified: May 8, 2019
This is version 165 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again