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Entry version 143 (11 Dec 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Vascular endothelial growth factor receptor 2

Gene

KDR

Organism
Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
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/or VEGFD and plays an essential role in the regulation of angiogenesis and vascular development. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Binding of vascular growth factors 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 (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei859ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei1021Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi831 – 839ATPPROSITE-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 1673

<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%5Fand%5Ftaxonomy%5Fsection">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):
Endothelial kinase receptor EK1
Quek 1
Short name:
Quek1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:EK1, FLK-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiCoturnix japonica (Japanese quail) (Coturnix coturnix japonica)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri93934 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePerdicinaeCoturnix

<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%5Flocation%5Fsection">'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 domaini21 – 756ExtracellularSequence analysisAdd BLAST736
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei757 – 777HelicalSequence analysisAdd BLAST21
Topological domaini778 – 1348CytoplasmicSequence analysisAdd BLAST571

Keywords - Cellular componenti

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

<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 – 20Sequence analysisAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001677421 – 1348Vascular endothelial growth factor receptor 2Add BLAST1328

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi43N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi47N-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 bondi50 ↔ 100PROSITE-ProRule annotation
Glycosylationi63N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi138N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi145 ↔ 195PROSITE-ProRule annotation
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi201N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi240N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi241 ↔ 299PROSITE-ProRule annotation
Glycosylationi290N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi310N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi365N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi386N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi436 ↔ 520PROSITE-ProRule annotation
Glycosylationi513N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi556N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi561 ↔ 633PROSITE-ProRule annotation
Glycosylationi603N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi613N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi622N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi666N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi679 ↔ 728PROSITE-ProRule annotation
Glycosylationi688N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi710N-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 residuei1047Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1052Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1168Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1207Phosphotyrosine; by autocatalysisBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

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 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P52583

<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

In all endothelial tissues during onset of vascularization. In later development, present in lung, heart, intestine and skin.

<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 whole mesoderm at onset of gastrulation. From day 2, confined to endothelial tissues and expression continues to be widespread throughout vascularization until E9 where it becomes restricted to specific regions such as the spinal chord and heart valves.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

In vitro, it is induced by basic fibroblast growth factor (bFGF), uniquely in the first 24 hours of cell culture.

<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

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-450N

<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
P52583

Database of comparative protein structure models

More...
ModBasei
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%5Fand%5Fdomains%5Fsection">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>Domaini43 – 106Ig-like C2-type 1Add BLAST64
Domaini138 – 202Ig-like C2-type 2Add BLAST65
Domaini220 – 312Ig-like C2-type 3Add BLAST93
Domaini320 – 405Ig-like C2-type 4Add BLAST86
Domaini412 – 534Ig-like C2-type 5Add BLAST123
Domaini540 – 651Ig-like C2-type 6Add BLAST112
Domaini658 – 744Ig-like C2-type 7Add BLAST87
Domaini825 – 1155Protein kinasePROSITE-ProRule annotationAdd BLAST331

<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 VEGF 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

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
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
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, 4 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P52583-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELGPLRVLT VLLCLAPVFA GLFISMDQPT LSIQKSVLTI TTNDTLNITC
60 70 80 90 100
SGQRAVYWSW PNNQSSVEKR LAVTGCSEGP FCKTLTLLRV IGNDTGDYRC
110 120 130 140 150
LYGDSQAATT IYVYVQDYRS PFVTSVGDQL GIVYITKNKT VVVPCLGTVS
160 170 180 190 200
NLNVSLHAKY PEKVFVPDGK SISWDNKKGF TIPSHLINYA GMVFCEAKID
210 220 230 240 250
NESYQSVIYI VAVVGYRIYD LTMNPHYQVE LAVGEKLVLN CTVRTELNVG
260 270 280 290 300
IDFRWDYPSI KERRATIRDL KTTAGEIKTF VSTLTIESVN LSDKGRYTCA
310 320 330 340 350
ASSGRMNMKN SSYFIIHESP FIHLEKMENV VEMKLGDTVS IPVKFKGYPP
360 370 380 390 400
PEAKWYKNGK VINANHTVKL GYALVITEAT EKDAGNYTVV LTNPTNKMQK
410 420 430 440 450
RHTFTLLVNV PPQIGENALM APVDSYKYGS TQALTCTIYA VPPPAAVLWY
460 470 480 490 500
WQLEEECTFS PQKVRLGANP YACRKWKVIS ERKGGNQVEI KQRVVTIAGK
510 520 530 540 550
TKTVSTLVIQ AANVSALYRC MATNRAGSSE RVISFHVTRG LEINLQPRSQ
560 570 580 590 600
LTEKDNTSLQ CTADKFTFEK LSWYKLSTHV SQTPFGGLPM PVCKNLDALQ
610 620 630 640 650
KLNATVSNVN GENVTLELIL RNISLQDGGD YVCIAQDKKA KTQHCLVKHL
660 670 680 690 700
TVQEPLHPRL VGNLENQTTN IGETIEVLCT VNGVPPPNIT WFKNSETLFE
710 720 730 740 750
DSGIVLKDGN KTLTIRRVRK EDGGLYTCLA CNILGCKKAE AFFSVQGAEE
760 770 780 790 800
KTNLELIILV GTAVIAMFFW LLLVIILRTV KRANGGDMKT GYLSIIMDPD
810 820 830 840 850
EVPIDEHCER LPYDASKWEF PRDRLKLGKP LGRGAFGQVI EADAFGIDKT
860 870 880 890 900
ATCRTVAVKM LKEGATHSEH RALMSELKIL IHIGHHLNVV NLLGACTKPG
910 920 930 940 950
GPLMVIVEYC KFGNLSAYLR SKRSEFIPYK MKSARFRQGK ENYTGDISTD
960 970 980 990 1000
LKQRLDSITS SQSSTSSGFV EERSLSDVEE EDAGSEDLCK NPLTMEDLIC
1010 1020 1030 1040 1050
YSFQVARGME FLASRKCIHR DLAARNILLS DNNVVKICDF GLARDIYKDP
1060 1070 1080 1090 1100
DYVRKGDARL PLKWMAPETI FDRVYTIQSD VWSFGVLLWE IFSLGASPYP
1110 1120 1130 1140 1150
GVKIDEEFCR RLKEGTRMRA PDYTTPEMYQ TMLDCWHGDP KQRPTFSELV
1160 1170 1180 1190 1200
EHLGNLLQAN VRQDGKDYVV LPLSVSLNME EDSGLSLPTS PASCKEEEEV
1210 1220 1230 1240 1250
CDPKFHYDNT AGISQYRQGS KRKSRPVSVK TFEDIPLVTT VKVVQEENQT
1260 1270 1280 1290 1300
DSGMVLASEE LKTLEEQDKQ VKIPFSTLAP SKSNESVMSE ASNQTSGYQS
1310 1320 1330 1340
GYHSDDMDNM VCSSEDTELL CAQEASPTLP RCAWPGIYSP APVASLPL
Length:1,348
Mass (Da):150,306
Last modified:October 1, 1996 - 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:iA5E4194A76FD5FB3
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 conflicti865A → S in AAB34594 (PubMed:7781909).Curated1

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
X83288 mRNA Translation: CAA58268.1
S65205 mRNA Translation: AAB28127.1
S78345 mRNA Translation: AAB34594.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4953 S51656

<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
X83288 mRNA Translation: CAA58268.1
S65205 mRNA Translation: AAB28127.1
S78345 mRNA Translation: AAB34594.1
PIRiJC4953 S51656

3D structure databases

SMRiP52583
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-450N

Proteomic databases

PRIDEiP52583

Enzyme and pathway databases

BRENDAi2.7.10.1 1673

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
IPR041348 VEGFR-2_TMD
IPR009136 VEGFR2_rcpt
PANTHERiPTHR24416:SF45 PTHR24416:SF45, 1 hit
PfamiView protein in Pfam
PF07679 I-set, 2 hits
PF07714 Pkinase_Tyr, 1 hit
PF17988 VEGFR-2_TMD, 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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_COTJA
<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: P52583
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 11, 2019
This is version 143 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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