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UniProtKB - P17948 (VGFR1_HUMAN)

Entry version 225 (08 May 2019)
Sequence version 2 (03 Apr 2007)
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Protein

Vascular endothelial growth factor receptor 1

Gene

FLT1

Organism
Homo sapiens (Human)
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, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). 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. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. 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 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 and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion.18 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.

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 sitei861ATPPROSITE-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 bindingi833 – 841ATPPROSITE-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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-194306 Neurophilin interactions with VEGF and VEGFR
R-HSA-195399 VEGF binds to VEGFR leading to receptor dimerization

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P17948

SIGNOR Signaling Network Open Resource

More...SIGNORi		P17948

<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):
Fms-like tyrosine kinase 1
Short name:
FLT-1
Tyrosine-protein kinase FRT
Tyrosine-protein kinase receptor FLT
Short name:
FLT
Vascular permeability factor receptor
<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:FLT, FRT, 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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 13

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3763 FLT1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		165070 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P17948

<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 domaini27 – 758ExtracellularSequence analysisAdd BLAST732
<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>Transmembranei759 – 780HelicalSequence analysisAdd BLAST22
Topological domaini781 – 1338CytoplasmicSequence analysisAdd BLAST558

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages.
Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi767V → A: Abolishes proteolytic cleavage by PSEN1. 1 Publication1
Mutagenesisi861K → M: Abolishes enzyme activity. Abolishes interaction with PLCG. 1 Publication1
Mutagenesisi914Y → F: Reduces phosphorylation at other tyrosine residues. 1 Publication1
Mutagenesisi1050N → D: Strongly increases kinase activity. Increases activity in promoting proliferation of endothelial cells. 1 Publication1
Mutagenesisi1169Y → F: Loss of phosphorylation site. Abolishes interaction with PLCG. 1 Publication1
Mutagenesisi1213Y → F: Loss of phosphorylation site. Abolishes interaction with PIK3R1. 1 Publication1
Mutagenesisi1242Y → F: Loss of phosphorylation site. 1 Publication1
Mutagenesisi1327Y → F: Loss of phosphorylation site. 1 Publication1
Mutagenesisi1333Y → F: Loss of phosphorylation site. Abolishes interaction with CBL. 2 Publications1

Organism-specific databases

DisGeNET

More...DisGeNETi		2321

MalaCards human disease database

More...MalaCardsi		FLT1

Open Targets

More...OpenTargetsi		ENSG00000102755

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		275555 Preeclampsia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28180

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1868

Drug and drug target database

More...DrugBanki		DB06080 ABT-869
DB06626 Axitinib
DB06101 IMC-1C11
DB09078 Lenvatinib
DB07288 N-(4-chlorophenyl)-2-[(pyridin-4-ylmethyl)amino]benzamide
DB09079 Nintedanib
DB05913 OSI-930
DB06589 Pazopanib
DB08896 Regorafenib
DB00398 Sorafenib
DB01268 Sunitinib
DB05075 TG100801
DB04879 Vatalanib

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1812

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FLT1

Domain mapping of disease mutations (DMDM)

More...DMDMi		143811474

<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 – 261 PublicationAdd BLAST26
<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_000001676827 – 1338Vascular endothelial growth factor receptor 1Add BLAST1312

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 ↔ 107PROSITE-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>Glycosylationi100N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi158 ↔ 207
Glycosylationi164N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi196N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi251N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi252 ↔ 311PROSITE-ProRule annotation
Glycosylationi323N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi402N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi417N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi454 ↔ 535PROSITE-ProRule annotation
Glycosylationi474N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi547N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi577 ↔ 636PROSITE-ProRule annotation
Glycosylationi597N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi620N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi625N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi666N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi682 ↔ 731PROSITE-ProRule annotation
<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 residuei914Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1053Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1169Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1213Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei1242Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1309Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei1327Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei1333Phosphotyrosine; by autocatalysis1 Publication1

<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.2 Publications
Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation.1 Publication
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-1333 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei767 – 768Cleavage; by PSEN1Curated2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P17948

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P17948

MaxQB - The MaxQuant DataBase

More...MaxQBi		P17948

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

More...PaxDbi		P17948

PeptideAtlas

More...PeptideAtlasi		P17948

PRoteomics IDEntifications database

More...PRIDEi		P17948

ProteomicsDB human proteome resource

More...ProteomicsDBi		53530
53531 [P17948-2]
53532 [P17948-3]
53533 [P17948-4]
53534 [P17948-5]
53535 [P17948-6]
53536 [P17948-7]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		771

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P17948

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

More...PhosphoSitePlusi		P17948

UniCarbKB; an annotated and curated database of glycan structures

More...UniCarbKBi		P17948

<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

Detected in normal lung, but also in placenta, liver, kidney, heart and brain tissues. Specifically expressed in most of the vascular endothelial cells, and also expressed in peripheral blood monocytes. Isoform 2 is strongly expressed in placenta. Isoform 3 is expressed in corneal epithelial cells (at protein level). Isoform 3 is expressed in vascular smooth muscle cells (VSMC).2 Publications

<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

Up-regulated in coculture of VSMC/endothelial cell (EC) or by direct exposure to VEGF of VSMC monoculture. Up-regulated from the second trimester of pregnancy to the term and in the placenta of women with preeclampsia (PE). Up-regulated in monocytes exposed to bacterial lipopolysaccharide (LPS).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000102755 Expressed in 220 organ(s), highest expression level in placenta

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P17948 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P17948 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB068189
CAB068190
HPA011740
HPA014290

<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 (when tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts also with PTPRB. Interacts with RACK1. Identified in a complex with CBL and CD2AP.16 Publications

<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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108609, 14 interactors

Database of interacting proteins

More...DIPi		DIP-643N

Protein interaction database and analysis system

More...IntActi		P17948, 32 interactors

Molecular INTeraction database

More...MINTi		P17948

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000282397

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P17948

<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

Secondary structure

11338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FLTX-ray1.70X/Y132-226[»]
1QSVNMR-A129-229[»]
1QSZNMR-A129-229[»]
1QTYX-ray2.70T/U/X/Y129-229[»]
1RV6X-ray2.45X/Y130-229[»]
2XACX-ray2.71C/X129-226[»]
3HNGX-ray2.70A801-1158[»]
4CKVX-ray2.06X132-225[»]
4CL7X-ray2.00A/B/C/D132-225[»]
5ABDX-ray2.00E/I/X132-226[»]
5EX3X-ray2.41D827-835[»]
5T89X-ray4.00X/Y27-656[»]

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

More...SMRi		P17948

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P17948

<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 – 123Ig-like C2-type 1Add BLAST92
Domaini151 – 214Ig-like C2-type 2Add BLAST64
Domaini230 – 327Ig-like C2-type 3Add BLAST98
Domaini335 – 421Ig-like C2-type 4Add BLAST87
Domaini428 – 553Ig-like C2-type 5Add BLAST126
Domaini556 – 654Ig-like C2-type 6Add BLAST99
Domaini661 – 747Ig-like C2-type 7Add BLAST87
Domaini827 – 1158Protein kinasePROSITE-ProRule annotationAdd BLAST332

<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.2 Publications

<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

More...GeneTreei		ENSGT00940000158713

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000037949

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P17948

KEGG Orthology (KO)

More...KOi		K05096

Identification of Orthologs from Complete Genome Data

More...OMAi		IFINDTG

Database of Orthologous Groups

More...OrthoDBi		1377476at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P17948

TreeFam database of animal gene trees

More...TreeFami		TF325768

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
IPR013106 Ig_V-set
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS
IPR041348 VEGFR-2_TMD
IPR009135 VEGFR1_rcpt

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07679 I-set, 2 hits
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF17988 VEGFR-2_TMD, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01833 VEGFRECEPTR1

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 5 hits
SM00406 IGv, 2 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, 6 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00240 RECEPTOR_TYR_KIN_III, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (8+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.

This entry has 8 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P17948-1) [UniParc]FASTAAdd to basket
Also known as: Flt1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVSYWDTGVL LCALLSCLLL TGSSSGSKLK DPELSLKGTQ HIMQAGQTLH 
        60         70         80         90        100
LQCRGEAAHK WSLPEMVSKE SERLSITKSA CGRNGKQFCS TLTLNTAQAN 
       110        120        130        140        150
HTGFYSCKYL AVPTSKKKET ESAIYIFISD TGRPFVEMYS EIPEIIHMTE 
       160        170        180        190        200
GRELVIPCRV TSPNITVTLK KFPLDTLIPD GKRIIWDSRK GFIISNATYK 
       210        220        230        240        250
EIGLLTCEAT VNGHLYKTNY LTHRQTNTII DVQISTPRPV KLLRGHTLVL 
       260        270        280        290        300
NCTATTPLNT RVQMTWSYPD EKNKRASVRR RIDQSNSHAN IFYSVLTIDK 
       310        320        330        340        350
MQNKDKGLYT CRVRSGPSFK SVNTSVHIYD KAFITVKHRK QQVLETVAGK 
       360        370        380        390        400
RSYRLSMKVK AFPSPEVVWL KDGLPATEKS ARYLTRGYSL IIKDVTEEDA 
       410        420        430        440        450
GNYTILLSIK QSNVFKNLTA TLIVNVKPQI YEKAVSSFPD PALYPLGSRQ 
       460        470        480        490        500
ILTCTAYGIP QPTIKWFWHP CNHNHSEARC DFCSNNEESF ILDADSNMGN 
       510        520        530        540        550
RIESITQRMA IIEGKNKMAS TLVVADSRIS GIYICIASNK VGTVGRNISF 
       560        570        580        590        600
YITDVPNGFH VNLEKMPTEG EDLKLSCTVN KFLYRDVTWI LLRTVNNRTM 
       610        620        630        640        650
HYSISKQKMA ITKEHSITLN LTIMNVSLQD SGTYACRARN VYTGEEILQK 
       660        670        680        690        700
KEITIRDQEA PYLLRNLSDH TVAISSSTTL DCHANGVPEP QITWFKNNHK 
       710        720        730        740        750
IQQEPGIILG PGSSTLFIER VTEEDEGVYH CKATNQKGSV ESSAYLTVQG 
       760        770        780        790        800
TSDKSNLELI TLTCTCVAAT LFWLLLTLFI RKMKRSSSEI KTDYLSIIMD 
       810        820        830        840        850
PDEVPLDEQC ERLPYDASKW EFARERLKLG KSLGRGAFGK VVQASAFGIK 
       860        870        880        890        900
KSPTCRTVAV KMLKEGATAS EYKALMTELK ILTHIGHHLN VVNLLGACTK 
       910        920        930        940        950
QGGPLMVIVE YCKYGNLSNY LKSKRDLFFL NKDAALHMEP KKEKMEPGLE 
       960        970        980        990       1000
QGKKPRLDSV TSSESFASSG FQEDKSLSDV EEEEDSDGFY KEPITMEDLI 
      1010       1020       1030       1040       1050
SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN 
      1060       1070       1080       1090       1100
PDYVRKGDTR LPLKWMAPES IFDKIYSTKS DVWSYGVLLW EIFSLGGSPY 
      1110       1120       1130       1140       1150
PGVQMDEDFC SRLREGMRMR APEYSTPEIY QIMLDCWHRD PKERPRFAEL 
      1160       1170       1180       1190       1200
VEKLGDLLQA NVQQDGKDYI PINAILTGNS GFTYSTPAFS EDFFKESISA 
      1210       1220       1230       1240       1250
PKFNSGSSDD VRYVNAFKFM SLERIKTFEE LLPNATSMFD DYQGDSSTLL 
      1260       1270       1280       1290       1300
ASPMLKRFTW TDSKPKASLK IDLRVTSKSK ESGLSDVSRP SFCHSSCGHV 
      1310       1320       1330 
SEGKRRFTYD HAELERKIAC CSPPPDYNSV VLYSTPPI
Length:1,338
Mass (Da):150,769
Last modified:April 3, 2007 - v2
<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:iFF3381EEFAF0787C
GO
Isoform 2 (identifier: P17948-2) [UniParc]FASTAAdd to basket
Also known as: sFlt1

The sequence of this isoform differs from the canonical sequence as follows:
     657-687: DQEAPYLLRNLSDHTVAISSSTTLDCHANGV → GEHCNKKAVFSRISKFKSTRNDCTTQSNVKH
     688-1338: Missing.

Show »
Length:687
Mass (Da):77,474
Checksum:i3F73F4942469DA36
GO
Isoform 3 (identifier: P17948-3) [UniParc]FASTAAdd to basket
Also known as: sFlt1-14

The sequence of this isoform differs from the canonical sequence as follows:
     706-733: GIILGPGSSTLFIERVTEEDEGVYHCKA → ELYTSTSPSSSSSSPLSSSSSSSSSSSS
     734-1338: Missing.

Show »
Length:733
Mass (Da):82,124
Checksum:i67B7F8BC1D30CD9E
GO
Isoform 4 (identifier: P17948-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     518-541: MASTLVVADSRISGIYICIASNKV → LPPANSSFMLPPTSFSSNYFHFLP
     542-1338: Missing.

Show »
Length:541
Mass (Da):60,917
Checksum:i50BCDAACB69B0EA2
GO
Isoform 5 (identifier: P17948-5) [UniParc]FASTAAdd to basket
Also known as: i15

The sequence of this isoform differs from the canonical sequence as follows:
     1-782: Missing.

Show »
Length:556
Mass (Da):62,954
Checksum:i9150507FBDF43B24
GO
Isoform 6 (identifier: P17948-6) [UniParc]FASTAAdd to basket
Also known as: i18

The sequence of this isoform differs from the canonical sequence as follows:
     1-875: Missing.

Show »
Length:463
Mass (Da):52,613
Checksum:i7D3D572623A1124E
GO
Isoform 7 (identifier: P17948-7) [UniParc]FASTAAdd to basket
Also known as: i21

The sequence of this isoform differs from the canonical sequence as follows:
     1-995: Missing.

Show »
Length:343
Mass (Da):39,148
Checksum:iB7800AF7311BF0D6
GO
Isoform 8 (identifier: P17948-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MVSYWDT → MNSDLLV
     8-984: Missing.

Show »
Length:361
Mass (Da):41,175
Checksum:i34E2B38DE128BA53
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1W2PNW4A0A1W2PNW4_HUMAN
Vascular endothelial growth factor ...
FLT1
665Annotation 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>
H9N1E7H9N1E7_HUMAN
Vascular endothelial growth factor ...
FLT1
433Annotation 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>
H9N1E8H9N1E8_HUMAN
Vascular endothelial growth factor ...
FLT1
85Annotation 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 conflicti490F → S in AAC16449 (PubMed:10471394).Curated1
Sequence conflicti779F → L in CAA35946 (PubMed:2158038).Curated1
Sequence conflicti1029L → F in ABI53803 (PubMed:20512933).Curated1
Sequence conflicti1029L → F in ABI53804 (PubMed:20512933).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04204560K → T1 PublicationCorresponds to variant dbSNP:rs56409818Ensembl.1
Natural variantiVAR_049719128I → L. Corresponds to variant dbSNP:rs35073261Ensembl.1
Natural variantiVAR_042046144E → K1 PublicationCorresponds to variant dbSNP:rs55974987Ensembl.1
Natural variantiVAR_042047281R → Q1 PublicationCorresponds to variant dbSNP:rs55687105Ensembl.1
Natural variantiVAR_042048422L → I in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042049781R → Q in a glioma low grade oligodendroglioma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs553261958Ensembl.1
Natural variantiVAR_042050938M → V1 PublicationCorresponds to variant dbSNP:rs35549791Ensembl.1
Natural variantiVAR_042051982E → A1 PublicationCorresponds to variant dbSNP:rs35832528Ensembl.1
Natural variantiVAR_0420521061L → V in a bladder transitional cell carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0419831 – 995Missing in isoform 7. 1 PublicationAdd BLAST995
Alternative sequenceiVSP_0419841 – 875Missing in isoform 6. 1 PublicationAdd BLAST875
Alternative sequenceiVSP_0419851 – 782Missing in isoform 5. 1 PublicationAdd BLAST782
Alternative sequenceiVSP_0477591 – 7MVSYWDT → MNSDLLV in isoform 8. 1 Publication7
Alternative sequenceiVSP_0477608 – 984Missing in isoform 8. 1 PublicationAdd BLAST977
Alternative sequenceiVSP_041929518 – 541MASTL…ASNKV → LPPANSSFMLPPTSFSSNYF HFLP in isoform 4. 1 PublicationAdd BLAST24
Alternative sequenceiVSP_041930542 – 1338Missing in isoform 4. 1 PublicationAdd BLAST797
Alternative sequenceiVSP_002955657 – 687DQEAP…HANGV → GEHCNKKAVFSRISKFKSTR NDCTTQSNVKH in isoform 2. 3 PublicationsAdd BLAST31
Alternative sequenceiVSP_002956688 – 1338Missing in isoform 2. 3 PublicationsAdd BLAST651
Alternative sequenceiVSP_041927706 – 733GIILG…YHCKA → ELYTSTSPSSSSSSPLSSSS SSSSSSSS in isoform 3. 3 PublicationsAdd BLAST28
Alternative sequenceiVSP_041928734 – 1338Missing in isoform 3. 3 PublicationsAdd BLAST605

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
X51602 mRNA Translation: CAA35946.1
U01134 mRNA Translation: AAC50060.1
AF063657 mRNA Translation: AAC16449.2
EU826561 mRNA Translation: ACF47597.1
EU368830 mRNA Translation: ACA62948.1
DQ836394 mRNA Translation: ABI53803.1
DQ836395 mRNA Translation: ABI53804.1
DQ836396 mRNA Translation: ABI53805.1
EF491868 mRNA Translation: ABS32268.1
EF491869 mRNA Translation: ABS32269.1
EF491870 mRNA Translation: ABS32270.1
EU360600 mRNA Translation: ACB05747.1
EU332841 Genomic DNA Translation: ABY87530.1
AK292936 mRNA Translation: BAF85625.1
AK300392 mRNA Translation: BAG62125.1
AL138712 Genomic DNA No translation available.
AL139005 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08431.1
CH471075 Genomic DNA Translation: EAX08432.1
BC039007 mRNA Translation: AAH39007.1
D00133 Genomic DNA Translation: BAA00080.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS53860.1 [P17948-3]
CCDS53861.1 [P17948-4]
CCDS73556.1 [P17948-2]
CCDS9330.1 [P17948-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A49636
S09982

NCBI Reference Sequences

More...RefSeqi		NP_001153392.1, NM_001159920.1 [P17948-2]
NP_001153502.1, NM_001160030.1 [P17948-3]
NP_001153503.1, NM_001160031.1 [P17948-4]
NP_002010.2, NM_002019.4 [P17948-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000282397; ENSP00000282397; ENSG00000102755 [P17948-1]
ENST00000539099; ENSP00000442630; ENSG00000102755 [P17948-4]
ENST00000541932; ENSP00000437631; ENSG00000102755 [P17948-3]
ENST00000543394; ENSP00000437841; ENSG00000102755 [P17948-8]
ENST00000615840; ENSP00000484039; ENSG00000102755 [P17948-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2321

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2321

UCSC genome browser

More...UCSCi		uc001usb.4 human [P17948-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
X51602 mRNA Translation: CAA35946.1
U01134 mRNA Translation: AAC50060.1
AF063657 mRNA Translation: AAC16449.2
EU826561 mRNA Translation: ACF47597.1
EU368830 mRNA Translation: ACA62948.1
DQ836394 mRNA Translation: ABI53803.1
DQ836395 mRNA Translation: ABI53804.1
DQ836396 mRNA Translation: ABI53805.1
EF491868 mRNA Translation: ABS32268.1
EF491869 mRNA Translation: ABS32269.1
EF491870 mRNA Translation: ABS32270.1
EU360600 mRNA Translation: ACB05747.1
EU332841 Genomic DNA Translation: ABY87530.1
AK292936 mRNA Translation: BAF85625.1
AK300392 mRNA Translation: BAG62125.1
AL138712 Genomic DNA No translation available.
AL139005 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08431.1
CH471075 Genomic DNA Translation: EAX08432.1
BC039007 mRNA Translation: AAH39007.1
D00133 Genomic DNA Translation: BAA00080.1
CCDSiCCDS53860.1 [P17948-3]
CCDS53861.1 [P17948-4]
CCDS73556.1 [P17948-2]
CCDS9330.1 [P17948-1]
PIRiA49636
S09982
RefSeqiNP_001153392.1, NM_001159920.1 [P17948-2]
NP_001153502.1, NM_001160030.1 [P17948-3]
NP_001153503.1, NM_001160031.1 [P17948-4]
NP_002010.2, NM_002019.4 [P17948-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FLTX-ray1.70X/Y132-226[»]
1QSVNMR-A129-229[»]
1QSZNMR-A129-229[»]
1QTYX-ray2.70T/U/X/Y129-229[»]
1RV6X-ray2.45X/Y130-229[»]
2XACX-ray2.71C/X129-226[»]
3HNGX-ray2.70A801-1158[»]
4CKVX-ray2.06X132-225[»]
4CL7X-ray2.00A/B/C/D132-225[»]
5ABDX-ray2.00E/I/X132-226[»]
5EX3X-ray2.41D827-835[»]
5T89X-ray4.00X/Y27-656[»]
SMRiP17948
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108609, 14 interactors
DIPiDIP-643N
IntActiP17948, 32 interactors
MINTiP17948
STRINGi9606.ENSP00000282397

Chemistry databases

BindingDBiP17948
ChEMBLiCHEMBL1868
DrugBankiDB06080 ABT-869
DB06626 Axitinib
DB06101 IMC-1C11
DB09078 Lenvatinib
DB07288 N-(4-chlorophenyl)-2-[(pyridin-4-ylmethyl)amino]benzamide
DB09079 Nintedanib
DB05913 OSI-930
DB06589 Pazopanib
DB08896 Regorafenib
DB00398 Sorafenib
DB01268 Sunitinib
DB05075 TG100801
DB04879 Vatalanib
GuidetoPHARMACOLOGYi1812

PTM databases

GlyConnecti771
iPTMnetiP17948
PhosphoSitePlusiP17948
UniCarbKBiP17948

Polymorphism and mutation databases

BioMutaiFLT1
DMDMi143811474

Proteomic databases

EPDiP17948
jPOSTiP17948
MaxQBiP17948
PaxDbiP17948
PeptideAtlasiP17948
PRIDEiP17948
ProteomicsDBi53530
53531 [P17948-2]
53532 [P17948-3]
53533 [P17948-4]
53534 [P17948-5]
53535 [P17948-6]
53536 [P17948-7]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2321
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000282397; ENSP00000282397; ENSG00000102755 [P17948-1]
ENST00000539099; ENSP00000442630; ENSG00000102755 [P17948-4]
ENST00000541932; ENSP00000437631; ENSG00000102755 [P17948-3]
ENST00000543394; ENSP00000437841; ENSG00000102755 [P17948-8]
ENST00000615840; ENSP00000484039; ENSG00000102755 [P17948-2]
GeneIDi2321
KEGGihsa:2321
UCSCiuc001usb.4 human [P17948-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2321
DisGeNETi2321

GeneCards: human genes, protein and diseases

More...GeneCardsi		FLT1

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0130593
HGNCiHGNC:3763 FLT1
HPAiCAB068189
CAB068190
HPA011740
HPA014290
MalaCardsiFLT1
MIMi165070 gene
neXtProtiNX_P17948
OpenTargetsiENSG00000102755
Orphaneti275555 Preeclampsia
PharmGKBiPA28180

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000158713
HOGENOMiHOG000037949
InParanoidiP17948
KOiK05096
OMAiIFINDTG
OrthoDBi1377476at2759
PhylomeDBiP17948
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-194306 Neurophilin interactions with VEGF and VEGFR
R-HSA-195399 VEGF binds to VEGFR leading to receptor dimerization
SignaLinkiP17948
SIGNORiP17948

Miscellaneous databases

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

More...ChiTaRSi		FLT1 human
EvolutionaryTraceiP17948

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		FLT1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2321

Protein Ontology

More...PROi		PR:P17948

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000102755 Expressed in 220 organ(s), highest expression level in placenta
ExpressionAtlasiP17948 baseline and differential
GenevisibleiP17948 HS

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
IPR013106 Ig_V-set
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS
IPR041348 VEGFR-2_TMD
IPR009135 VEGFR1_rcpt
PfamiView protein in Pfam
PF07679 I-set, 2 hits
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF17988 VEGFR-2_TMD, 1 hit
PRINTSiPR01833 VEGFRECEPTR1
SMARTiView protein in SMART
SM00409 IG, 7 hits
SM00408 IGc2, 5 hits
SM00406 IGv, 2 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 7 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 6 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_HUMAN
<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: P17948
Secondary accession number(s): A3E342
, A3E344, A8KA71, B0LPF1, B2BF46, B2BF47, B2BF48, B3FR89, B5A923, F5H5L6, O60722, P16057, Q12954
<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: November 1, 1990
Last sequence update: April 3, 2007
Last modified: May 8, 2019
This is version 225 of the entry and version 2 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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