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Entry version 191 (16 Oct 2019)
Sequence version 1 (01 Jun 1994)
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Protein

Vascular endothelial growth factor receptor 3

Gene

Flt4

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 VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'.6 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 <a href="http://www.uniprot.org/help/function_section">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 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_section">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 sitei879ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei1037Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi851 – 859ATPPROSITE-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 functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processAngiogenesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 3474

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-MMU-195399 VEGF binds to VEGFR leading to receptor dimerization

<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 3 (EC:2.7.10.1)
Short name:
VEGFR-3
Alternative name(s):
Fms-like tyrosine kinase 4
Short name:
FLT-4
Tyrosine-protein kinase receptor FLT4
<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:Flt4
Synonyms:Flt-4, Vegfr3
<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: Chromosome 11

Organism-specific databases

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

More...
MGIi
MGI:95561 Flt4

<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 domaini25 – 775ExtracellularSequence analysisAdd BLAST751
<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>Transmembranei776 – 796HelicalSequence analysisAdd BLAST21
Topological domaini797 – 1363CytoplasmicSequence analysisAdd BLAST567

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

<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 about 13 dpc, due to failure of remodeling of the yolk sac capillary network and defects in remodeling and maturation of primary vascular networks.1 Publication

Chemistry databases

DrugCentral

More...
DrugCentrali
P35917

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
1814

<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 – 24Sequence analysisAdd BLAST24
<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_000001677725 – 1363Vascular endothelial growth factor receptor 3Add BLAST1339

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>Glycosylationi33N-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 bondi51 ↔ 111PROSITE-ProRule annotation
Glycosylationi104N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi158 ↔ 206PROSITE-ProRule annotation
Glycosylationi166N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi251N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi252 ↔ 310PROSITE-ProRule annotation
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi411N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi445 ↔ 534PROSITE-ProRule annotation
Disulfide bondi466 ↔ 486By similarity
Glycosylationi515N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi527N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi578 ↔ 653PROSITE-ProRule annotation
Glycosylationi582N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi594N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi683N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi690N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi699 ↔ 751PROSITE-ProRule annotation
Glycosylationi758N-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 residuei830Phosphotyrosine; by SRCBy similarity1
Modified residuei833Phosphotyrosine; by SRCBy similarity1
Modified residuei1063Phosphotyrosine; by autocatalysis and SRCBy similarity1
Modified residuei1068Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1230Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1231Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1265Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1333Phosphotyrosine; by autocatalysis and SRCBy similarity1
Modified residuei1337Phosphotyrosine; by autocatalysis and SRCBy similarity1
Modified residuei1363Phosphotyrosine; 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

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 in response to H2O2 is mediated by a process that requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is required for autophosphorylation at additional tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction with CRK and subsequent activation of MAPK8. Phosphorylation at Tyr-1230, Tyr-1231 and Tyr-1337 is important for interaction with GRB2 and subsequent activation of the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1 signaling pathways. In response to endothelial cell adhesion onto collagen, can also be phosphorylated in the absence of FLT4 kinase activity by SRC (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3753

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

More...
PaxDbi
P35917

PeptideAtlas

More...
PeptideAtlasi
P35917

PRoteomics IDEntifications database

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PRIDEi
P35917

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35917

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

More...
PhosphoSitePlusi
P35917

<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 adult lung and liver, and in fetal liver, brain, intestine and placenta.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000020357 Expressed in 229 organ(s), highest expression level in endothelial cell of lymphatic vessel

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P35917 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35917 MM

<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

Interacts with VEGFC and VEGFD. Monomer in the absence of bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or VEGFD. Can also form a heterodimer with KDR.

Interacts with PTPN14; the interaction is enhanced by stimulation with VEGFC.

Interacts with CRK, GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-2.

Identified in a complex with SRC and ITGB1 (By similarity).

By similarity

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199709, 5 interactors

Database of interacting proteins

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DIPi
DIP-60714N

Protein interaction database and analysis system

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IntActi
P35917, 3 interactors

Molecular INTeraction database

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MINTi
P35917

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000020617

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P35917

<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

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SMRi
P35917

Database of comparative protein structure models

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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_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>Domaini44 – 118Ig-like C2-type 1Add BLAST75
Domaini151 – 213Ig-like C2-type 2Add BLAST63
Domaini230 – 326Ig-like C2-type 3Add BLAST97
Domaini331 – 415Ig-like C2-type 4Add BLAST85
Domaini422 – 552Ig-like C2-type 5Add BLAST131
Domaini555 – 671Ig-like C2-type 6Add BLAST117
Domaini678 – 764Ig-like C2-type 7Add BLAST87
Domaini845 – 1173Protein 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 first and second Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding. The fourth and fifth Ig-like C2-type (immunoglobulin-like) domains are sufficient for homodimerization. The fifth and seventh Ig-like C2-type (immunoglobulin-like) domains are required for autophosphorylation and further activation.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

Ensembl GeneTree

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GeneTreei
ENSGT00940000159358

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000037949

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35917

KEGG Orthology (KO)

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KOi
K05097

Identification of Orthologs from Complete Genome Data

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OMAi
NQRGCVH

Database of Orthologous Groups

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OrthoDBi
236292at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35917

TreeFam database of animal gene trees

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TreeFami
TF325768

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
IPR041348 VEGFR-2_TMD
IPR009137 VEGFR3_rcpt

The PANTHER Classification System

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PANTHERi
PTHR24416:SF49 PTHR24416:SF49, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF07679 I-set, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF17988 VEGFR-2_TMD, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 6 hits
SM00408 IGc2, 4 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48726 SSF48726, 5 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>. 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_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.

P35917-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQPGAALNLR LWLCLGLLQG LANGYSMTPP TLNITEDSYV IDTGDSLSIS
60 70 80 90 100
CRGQHPLEWT WPGAQEVLTT GGKDSEDTRV VHDCEGTEAR PYCKVLLLAQ
110 120 130 140 150
THANNTGSYH CYYKYIKARI EGTTAASTYV FVRDFKHPFI NKPDTLLVNR
160 170 180 190 200
KDSMWVPCLV SIPGLNITLR SQSSALHPDG QEVLWDDRRG MRVPTQLLRD
210 220 230 240 250
ALYLQCETTW GDQNFLSNLF VVHITGNELY DIQLYPKKSM ELLVGEKLVL
260 270 280 290 300
NCTVWAEFDS GVTFDWDYPG KQAERAKWVP ERRSQQTHTE LSSILTIHNV
310 320 330 340 350
SQNDLGPYVC EANNGIQRFR ESTEVIVHEK PFISVEWLKG PVLEATAGDE
360 370 380 390 400
LVKLPVKLAA YPPPEFQWYK DRKAVTGRHN PHALVLKEVT EASAGVYTLA
410 420 430 440 450
LWNSAAGLRQ NISLELVVNV PPHIHEKEAS SPSIYSRHSR QTLTCTAYGV
460 470 480 490 500
PQPLSVQWHW RPWTPCKTFA QRSLRRRQQR DGMPQCRDWK EVTTQDAVNP
510 520 530 540 550
IESLDSWTEF VEGKNKTVSK LVIQDANVSA MYKCVVVNKV GQDERLIYFY
560 570 580 590 600
VTTIPDGFSI ESEPSEDPLE GQSVRLSCRA DNYTYEHLRW YRLNLSTLHD
610 620 630 640 650
AQGNPLLLDC KNVHLFATPL EANLEEAEPG ARHATLSLNI PRVAPEDEGD
660 670 680 690 700
YVCEVQDRRS QDKHCHKKYL SVQALEAPRL TQNLTDLLVN VSDSLEMRCP
710 720 730 740 750
VAGAHVPSIV WYKDERLLEK ESGIDLADSN QRLSIQRVRE EDAGRYLCSV
760 770 780 790 800
CNAKGCVNSS ASVAVEGSED KGSMEIVILI GTGVIAVFFW VLLLLIFCNM
810 820 830 840 850
KRPAHADIKT GYLSIIMDPG EVPLEEQCEY LSYDASQWEF PRERLHLGRV
860 870 880 890 900
LGHGAFGKVV EASAFGINKG SSCDTVAVKM LKEGATASEH RALMSELKIL
910 920 930 940 950
IHIGNHLNVV NLLGACTKPN GPLMVIVEFC KYGNLSNFLR VKRDTFNPYA
960 970 980 990 1000
EKSPEQRRRF RAMVEGAKAD RRRPGSSDRA LFTRFLMGKG SARRAPLVQE
1010 1020 1030 1040 1050
AEDLWLSPLT MEDLVCYSFQ VARGMEFLAS RKCIHRDLAA RNILLSESDI
1060 1070 1080 1090 1100
VKICDFGLAR DIYKDPDYVR KGSARLPLKW MAPESIFDKV YTTQSDVWSF
1110 1120 1130 1140 1150
GVLLWEIFSL GASPYPGVQI NEEFCQRLKD GTRMRAPELA TPAIRHIMQS
1160 1170 1180 1190 1200
CWSGDPKARP AFSDLVEILG DLLQGGGWQE EEEERMALHS SQSSEEDGFM
1210 1220 1230 1240 1250
QASTTALHIT EADADDSPPS MHCHSLAARY YNCVSFPGRL ARGTKTPGSS
1260 1270 1280 1290 1300
RMKTFEELPM TPTTYKASMD NQTDSGMVLA SEEFEELESR HRPEGSFSCK
1310 1320 1330 1340 1350
GPGQHMDIPR GHPDPQGRRR RPTQGAQGGK VFYNNEYGEV SQPCTEGDCC
1360
PSAGSTFFAD SSY
Length:1,363
Mass (Da):153,016
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:iF1BF8A2BDEF99BE9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
L07296 mRNA Translation: AAA40077.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS24618.1

Protein sequence database of the Protein Information Resource

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PIRi
I58375

NCBI Reference Sequences

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RefSeqi
NP_032055.1, NM_008029.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000020617; ENSMUSP00000020617; ENSMUSG00000020357

Database of genes from NCBI RefSeq genomes

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GeneIDi
14257

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:14257

UCSC genome browser

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UCSCi
uc007iqu.2 mouse

<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
L07296 mRNA Translation: AAA40077.1
CCDSiCCDS24618.1
PIRiI58375
RefSeqiNP_032055.1, NM_008029.3

3D structure databases

SMRiP35917
ModBaseiSearch...

Protein-protein interaction databases

BioGridi199709, 5 interactors
DIPiDIP-60714N
IntActiP35917, 3 interactors
MINTiP35917
STRINGi10090.ENSMUSP00000020617

Chemistry databases

BindingDBiP35917
DrugCentraliP35917
GuidetoPHARMACOLOGYi1814

PTM databases

iPTMnetiP35917
PhosphoSitePlusiP35917

Proteomic databases

CPTACinon-CPTAC-3753
PaxDbiP35917
PeptideAtlasiP35917
PRIDEiP35917

Genome annotation databases

EnsembliENSMUST00000020617; ENSMUSP00000020617; ENSMUSG00000020357
GeneIDi14257
KEGGimmu:14257
UCSCiuc007iqu.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2324
MGIiMGI:95561 Flt4

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000159358
HOGENOMiHOG000037949
InParanoidiP35917
KOiK05097
OMAiNQRGCVH
OrthoDBi236292at2759
PhylomeDBiP35917
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 3474
ReactomeiR-MMU-195399 VEGF binds to VEGFR leading to receptor dimerization

Miscellaneous databases

Protein Ontology

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PROi
PR:P35917

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020357 Expressed in 229 organ(s), highest expression level in endothelial cell of lymphatic vessel
ExpressionAtlasiP35917 baseline and differential
GenevisibleiP35917 MM

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
IPR009137 VEGFR3_rcpt
PANTHERiPTHR24416:SF49 PTHR24416:SF49, 1 hit
PfamiView protein in Pfam
PF07679 I-set, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF17988 VEGFR-2_TMD, 1 hit
SMARTiView protein in SMART
SM00409 IG, 6 hits
SM00408 IGc2, 4 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 5 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 5 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00240 RECEPTOR_TYR_KIN_III, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiVGFR3_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: P35917
<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: October 16, 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
UniProt is an ELIXIR core data resource
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