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

Vascular endothelial growth factor receptor 1

Gene

Flt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, and proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts. Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to the activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC, YES1 and PLCG, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 and PTK2/FAK1 (By similarity).By similarity6 Publications

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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFB or PGF 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 ‘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 sitei862ATPPROSITE-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 sitei1022Proton 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 bindingi834 – 842ATPPROSITE-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, Chemotaxis, Differentiation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 3474

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Vascular endothelial growth factor receptor 1 (EC:2.7.10.1)
Short name:
VEGFR-1
Alternative name(s):
Embryonic receptor kinase 2
Fms-like tyrosine kinase 1
Short name:
FLT-1
Tyrosine-protein kinase receptor FLT
<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:Flt1
Synonyms:Emrk2, Flt, Vegfr1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

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

More...
MGIi
MGI:95558 Flt1

<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 domaini23 – 759ExtracellularSequence analysisAdd BLAST737
<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>Transmembranei760 – 781HelicalSequence analysisAdd BLAST22
Topological domaini782 – 1333CytoplasmicSequence analysisAdd BLAST552

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

<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 9 dpc, due to defects in the formation and organization of the vascular network. Mice display abnormal blood island structures in the yolk sac, leading to defects in the organization of the vascular endothelium, excess growth and disorganization of embryonic and extraembryonic vasculature, including the endocardium and the microvasculature. Mice expressing a mutant protein that lacks the kinase domain survive and have no apparent phenotype.3 Publications

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3516

<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 – 22Sequence analysisAdd BLAST22
<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_000001676923 – 1333Vascular endothelial growth factor receptor 1Add BLAST1311

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 ↔ 108PROSITE-ProRule annotation
<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>Glycosylationi101N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi159 ↔ 208PROSITE-ProRule annotation
Glycosylationi165N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi197N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi252N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi253 ↔ 312PROSITE-ProRule annotation
Glycosylationi324N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi418N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi455 ↔ 536PROSITE-ProRule annotation
Glycosylationi475N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi517N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi578 ↔ 637PROSITE-ProRule annotation
Glycosylationi598N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi626N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi667N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi683 ↔ 732PROSITE-ProRule annotation
Glycosylationi714N-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 residuei915Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1053Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1169Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1213Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1242Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1322Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1328Phosphotyrosine; 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 after VEGFA-mediated autophosphorylation, leading to proteolytic degradation.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-1169 is important for interaction with PLCG. Phosphorylation at Tyr-1213 is important for interaction with PIK3R1, PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1328 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB (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>Sitei768 – 769Cleavage; by PSEN1By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P35969

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

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PaxDbi
P35969

PeptideAtlas

More...
PeptideAtlasi
P35969

PRoteomics IDEntifications database

More...
PRIDEi
P35969

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35969

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

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PhosphoSitePlusi
P35969

<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 VEGFA, VEGFB and PGF. Monomer in the absence of bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA, VEGFB and PGF. Can also form a heterodimer with KDR. Interacts (tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts with PTPRB. Interacts with RACK1. Identified in a complex with CBL and CD2AP (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
199706, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P35969

Database of interacting proteins

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DIPi
DIP-39359N

Protein interaction database and analysis system

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IntActi
P35969, 9 interactors

Molecular INTeraction database

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MINTi
P35969

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000031653

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35969

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P35969

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

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SMRi
P35969

Database of comparative protein structure models

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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>Domaini32 – 124Ig-like C2-type 1Add BLAST93
Domaini152 – 215Ig-like C2-type 2Add BLAST64
Domaini231 – 328Ig-like C2-type 3Add BLAST98
Domaini334 – 429Ig-like C2-type 4Add BLAST96
Domaini430 – 550Ig-like C2-type 5Add BLAST121
Domaini557 – 656Ig-like C2-type 6Add BLAST100
Domaini662 – 748Ig-like C2-type 7Add BLAST87
Domaini828 – 1158Protein 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 VEGFA binding.By similarity

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

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

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000037949

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053432

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35969

KEGG Orthology (KO)

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KOi
K05096

Database of Orthologous Groups

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OrthoDBi
236292at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35969

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
IPR009135 VEGFR1_rcpt

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01833 VEGFRECEPTR1

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 6 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48726 SSF48726, 7 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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

P35969-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSCWDTAVL PYALLGCLLL TGYGSGSKLK VPELSLKGTQ HVMQAGQTLF
60 70 80 90 100
LKCRGEAAHS WSLPTTVSQE DKRLSITPPS ACGRDNRQFC STLTLDTAQA
110 120 130 140 150
NHTGLYTCRY LPTSTSKKKK AESSIYIFVS DAGSPFIEMH TDIPKLVHMT
160 170 180 190 200
EGRQLIIPCR VTSPNVTVTL KKFPFDTLTP DGQRITWDSR RGFIIANATY
210 220 230 240 250
KEIGLLNCEA TVNGHLYQTN YLTHRQTNTI LDVQIRPPSP VRLLHGQTLV
260 270 280 290 300
LNCTATTELN TRVQMSWNYP GKATKRASIR QRIDRSHSHN NVFHSVLKIN
310 320 330 340 350
NVESRDKGLY TCRVKSGSSF QSFNTSVHVY EKGFISVKHR KQPVQETTAG
360 370 380 390 400
RRSYRLSMKV KAFPSPEIVW LKDGSPATLK SARYLVHGYS LIIKDVTTED
410 420 430 440 450
AGDYTILLGI KQSRLFKNLT ATLIVNVKPQ IYEKSVSSLP SPPLYPLGSR
460 470 480 490 500
QVLTCTVYGI PRPTITWLWH PCHHNHSKER YDFCTENEES FILDPSSNLG
510 520 530 540 550
NRIESISQRM TVIEGTNKTV STLVVADSQT PGIYSCRAFN KIGTVERNIK
560 570 580 590 600
FYVTDVPNGF HVSLEKMPAE GEDLKLSCVV NKFLYRDITW ILLRTVNNRT
610 620 630 640 650
MHHSISKQKM ATTQDYSITL NLVIKNVSLE DSGTYACRAR NIYTGEDILR
660 670 680 690 700
KTEVLVRDSE APHLLQNLSD YEVSISGSTT LDCQARGVPA PQITWFKNNH
710 720 730 740 750
KIQQEPGIIL GPGNSTLFIE RVTEEDEGVY RCRATNQKGA VESAAYLTVQ
760 770 780 790 800
GTSDKSNLEL ITLTCTCVAA TLFWLLLTLF IRKLKRSSSE VKTDYLSIIM
810 820 830 840 850
DPDEVPLDEQ CERLPYDASK WEFARERLKL GKSLGRGAFG KVVQASAFGI
860 870 880 890 900
KKSPTCRTVA VKMLKEGATA SEYKALMTEL KILTHIGHHL NVVNLLGACT
910 920 930 940 950
KQGGPLMVIV EYCKYGNLSN YLKSKRDLFC LNKDAALHME LKKESLEPGL
960 970 980 990 1000
EQGQKPRLDS VSSSSVTSSS FPEDRSVSDV EGDEDYSEIS KQPLTMEDLI
1010 1020 1030 1040 1050
SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN
1060 1070 1080 1090 1100
PDYVRRGDTR LPLKWMAPES IFDKVYSTKS DVWSYGVLLW EIFSLGGSPY
1110 1120 1130 1140 1150
PGVQMDEDFC SRLKEGMRMR TPEYATPEIY QIMLDCWHKD PKERPRFAEL
1160 1170 1180 1190 1200
VEKLGDLLQA NVQQDGKDYI PLNAILTRNS SFTYSTPTFS EDLFKDGFAD
1210 1220 1230 1240 1250
PHFHSGSSDD VRYVNAFKFM SLERIKTFEE LSPNSTSMFE DYQLDTSTLL
1260 1270 1280 1290 1300
GSPLLKRFTW TETKPKASMK IDLRIASKSK EAGLSDLPRP SFCFSSCGHI
1310 1320 1330
RPVQDDESEL GKESCCSPPP DYNSVVLYSS PPA
Length:1,333
Mass (Da):149,876
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:iC06533B7ECBC404C
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
A0A0R4J0A4A0A0R4J0A4_MOUSE
Vascular endothelial growth factor ...
Flt1
1,333Annotation score:

Annotation score:3 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>
O55095O55095_MOUSE
SFlt-1
Flt1
688Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti158Missing in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti211Missing in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti245H → L in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti603H → N in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti609 – 615KMATTQD → NGHHSS in CAA55311 (PubMed:8134130).Curated7
Sequence conflicti696F → L in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti734A → S in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti765C → Y in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti820K → N in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti1009G → R in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti1181S → G in BAA24498 (PubMed:9524283).Curated1
Sequence conflicti1181S → N in CAA55311 (PubMed:8134130).Curated1
Sequence conflicti1193 – 1194LF → RG in CAA55311 (PubMed:8134130).Curated2
Sequence conflicti1278 – 1279KS → PR in CAA55311 (PubMed:8134130).Curated2

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

More...
DDBJi
Links Updated
L07297 mRNA Translation: AAA40078.1
X78568 mRNA Translation: CAA55311.1
D88689 mRNA Translation: BAA24498.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS19879.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I78875
S49010

NCBI Reference Sequences

More...
RefSeqi
NP_034358.2, NM_010228.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.389712
Mm.458302

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
14254

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:14254

UCSC genome browser

More...
UCSCi
uc009aoh.1 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
L07297 mRNA Translation: AAA40078.1
X78568 mRNA Translation: CAA55311.1
D88689 mRNA Translation: BAA24498.1
CCDSiCCDS19879.1
PIRiI78875
S49010
RefSeqiNP_034358.2, NM_010228.3
UniGeneiMm.389712
Mm.458302

3D structure databases

ProteinModelPortaliP35969
SMRiP35969
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199706, 4 interactors
CORUMiP35969
DIPiDIP-39359N
IntActiP35969, 9 interactors
MINTiP35969
STRINGi10090.ENSMUSP00000031653

Chemistry databases

BindingDBiP35969
ChEMBLiCHEMBL3516

PTM databases

iPTMnetiP35969
PhosphoSitePlusiP35969

Proteomic databases

MaxQBiP35969
PaxDbiP35969
PeptideAtlasiP35969
PRIDEiP35969

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi14254
KEGGimmu:14254
UCSCiuc009aoh.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2321
MGIiMGI:95558 Flt1

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
HOGENOMiHOG000037949
HOVERGENiHBG053432
InParanoidiP35969
KOiK05096
OrthoDBi236292at2759
PhylomeDBiP35969
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 3474

Miscellaneous databases

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

More...
ChiTaRSi
Flt1 mouse

Protein Ontology

More...
PROi
PR:P35969

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Family and domain databases

Gene3Di2.60.40.10, 7 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS
IPR009135 VEGFR1_rcpt
PfamiView protein in Pfam
PF07679 I-set, 2 hits
PF07714 Pkinase_Tyr, 1 hit
PRINTSiPR01833 VEGFRECEPTR1
SMARTiView protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 6 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 nameiVGFR1_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: P35969
Secondary accession number(s): O55094, Q61517
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 13, 2019
This is version 191 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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