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P35916 (VGFR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vascular endothelial growth factor receptor 3

Short name=VEGFR-3
EC=2.7.10.1
Alternative name(s):
Fms-like tyrosine kinase 4
Short name=FLT-4
Tyrosine-protein kinase receptor FLT4
Gene names
Name:FLT4
Synonyms:VEGFR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'. Ref.5 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.13 Ref.17

Enzyme regulation

Present in an inactive conformation in the absence of bound ligand. Binding of VEGFC or VEGFD leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by MAZ51. Ref.19 Ref.24 Ref.27

Subunit structure

Interacts with VEGFC and VEGFD. Monomer in the absence of bound VEGFC or VEGFD. Homodimer in the presence of bound VEGFC or VEGFD. Can also form a heterodimer with KDR. Interacts with PTPN14; the interaction is enhanced by stimulation with VEGFC. Interacts with CRK, GRB2, PTK2/FAK1, SHC1, PIK3R1 and PTPN11/SHP-2. Identified in a complex with SRC and ITGB1. Ref.5 Ref.6 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.25 Ref.26 Ref.27 Ref.28

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.6 Ref.13 Ref.22 Ref.29. Cytoplasm Ref.6 Ref.13 Ref.22 Ref.29. Nucleus. Note: Ligand-mediated autophosphorylation leads to rapid internalization. Ref.6 Ref.13 Ref.22 Ref.29

Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.6 Ref.13 Ref.22 Ref.29. Note: Ligand-mediated autophosphorylation leads to rapid internalization. Ref.6 Ref.13 Ref.22 Ref.29

Isoform 2: Cell membrane; Single-pass type I membrane protein Ref.6 Ref.13 Ref.22 Ref.29.

Isoform 3: Secreted. Cytoplasm Ref.6 Ref.13 Ref.22 Ref.29.

Tissue specificity

Detected in endothelial cells (at protein level). Widely expressed. Detected in fetal spleen, lung and brain. Detected in adult liver, muscle, thymus, placenta, lung, testis, ovary, prostate, heart, and kidney. Ref.1 Ref.14 Ref.28

Domain

The first and second Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFC binding.

Post-translational modification

Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation in response to H2O2 is mediated by a process that requires SRC and PRKCD activity. Phosphorylation at Tyr-1068 is required for autophosphorylation at additional tyrosine residues. Phosphorylation at Tyr-1063 and Tyr-1337 is important for interaction with CRK and subsequent activation of MAPK8. Phosphorylation at Tyr-1230, Tyr-1231 and Tyr-1337 is important for interaction with GRB2 and subsequent activation of the AKT1 and MAPK1/ERK2 and/or MAPK3/ERK1 signaling pathways. In response to endothelial cell adhesion onto collagen, can also be phosphorylated in the absence of FLT4 kinase activity by SRC at Tyr-830, Tyr-833, Tyr-853, Tyr-1063, Tyr-1333, and Tyr-1337. Ref.5 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.24 Ref.27

Involvement in disease

Lymphedema, hereditary, 1A (LMPH1A) [MIM:153100]: A chronic disabling condition which results in swelling of the extremities due to altered lymphatic flow. Patients with lymphedema suffer from recurrent local infections and physical impairment.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.19 Ref.35 Ref.36 Ref.37

Hemangioma, capillary infantile (HCI) [MIM:602089]: A condition characterized by dull red, firm, dome-shaped hemangiomas, sharply demarcated from surrounding skin, usually presenting at birth or occurring within the first two or three months of life. They result from highly proliferative, localized growth of capillary endothelium and generally undergo regression and involution without scarring.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.38

Plays an important role in tumor lymphangiogenesis, in cancer cell survival, migration, and formation of metastases.

Sequence similarities

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

Contains 7 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence caution

The sequence CAA48290.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to vascular endothelial growth factor stimulus

Inferred from direct assay Ref.15. Source: UniProtKB

lymph vessel development

Inferred from sequence or structural similarity. Source: BHF-UCL

lymphangiogenesis

Inferred from mutant phenotype Ref.24. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.16. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of JNK cascade

Inferred from mutant phenotype Ref.20. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from mutant phenotype Ref.24. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype Ref.24Ref.14. Source: UniProtKB

positive regulation of endothelial cell migration

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of protein kinase C signaling

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from mutant phenotype Ref.16Ref.24. Source: UniProtKB

positive regulation vascular endothelial growth factor production

Inferred from mutant phenotype Ref.24. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.14Ref.15. Source: UniProtKB

regulation of blood vessel remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

sprouting angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement Ref.37. Source: ProtInc

vascular endothelial growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.16Ref.24. Source: UniProtKB

vasculature development

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Traceable author statement Ref.4. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.13. Source: UniProtKB

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

growth factor binding

Inferred from physical interaction Ref.15. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction Ref.26. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

vascular endothelial growth factor-activated receptor activity

Inferred from mutant phenotype Ref.16Ref.24. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35916-2)

Also known as: Long;

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.
Isoform 2 (identifier: P35916-1)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1298-1363: SCKGPGQNVAVTRAHPDSQGRRRRPERGARGGQVFYNSEYGELSEPSEEDHCSPSARVTFFTDNSY → R
Isoform 3 (identifier: P35916-3)

Also known as: sVegfr3;

The sequence of this isoform differs from the canonical sequence as follows:
     724-765: VDLADSNQKL...CVNSSASVAV → REGGPGEGQV...ESTWRTPTRS
     766-1298: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.12
Chain25 – 13631339Vascular endothelial growth factor receptor 3
PRO_0000016776

Regions

Topological domain25 – 775751Extracellular Potential
Transmembrane776 – 79621Helical; Potential
Topological domain797 – 1363567Cytoplasmic Potential
Domain30 – 12798Ig-like C2-type 1
Domain151 – 21363Ig-like C2-type 2
Domain219 – 326108Ig-like C2-type 3
Domain331 – 41585Ig-like C2-type 4
Domain422 – 552131Ig-like C2-type 5
Domain555 – 671117Ig-like C2-type 6
Domain678 – 76487Ig-like C2-type 7
Domain845 – 1173329Protein kinase
Nucleotide binding851 – 8599ATP By similarity

Sites

Active site10371Proton acceptor By similarity
Binding site8791ATP Probable

Amino acid modifications

Modified residue8301Phosphotyrosine; by SRC Ref.27
Modified residue8331Phosphotyrosine; by SRC Ref.27
Modified residue8531Phosphotyrosine; by SRC Ref.27
Modified residue10631Phosphotyrosine; by autocatalysis and SRC Ref.20 Ref.27
Modified residue10681Phosphotyrosine; by autocatalysis Ref.20 Ref.27
Modified residue12301Phosphotyrosine; by autocatalysis Ref.17 Ref.20
Modified residue12311Phosphotyrosine; by autocatalysis Ref.17 Ref.20
Modified residue12651Phosphotyrosine; by autocatalysis Ref.17
Modified residue13331Phosphotyrosine; by autocatalysis and SRC Ref.17 Ref.27
Modified residue13371Phosphotyrosine; by autocatalysis and SRC Ref.17 Ref.20 Ref.27
Modified residue13631Phosphotyrosine; by autocatalysis Ref.17
Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation2511N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation4111N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation5271N-linked (GlcNAc...) Ref.21
Glycosylation5941N-linked (GlcNAc...) Potential
Glycosylation6831N-linked (GlcNAc...) Potential
Glycosylation6901N-linked (GlcNAc...) Potential
Glycosylation7581N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 111 By similarity
Disulfide bond158 ↔ 206 By similarity
Disulfide bond252 ↔ 310 By similarity
Disulfide bond445 ↔ 534 By similarity
Disulfide bond578 ↔ 653 By similarity
Disulfide bond699 ↔ 751 By similarity

Natural variations

Alternative sequence724 – 76542VDLAD…ASVAV → REGGPGEGQVRRPARPTIPN PGGPAPPPHPLQESTWRTPT RS in isoform 3.
VSP_041993
Alternative sequence766 – 1298533Missing in isoform 3.
VSP_041994
Alternative sequence1298 – 136366SCKGP…TDNSY → R in isoform 2.
VSP_041995
Natural variant1491N → D. Ref.39
Corresponds to variant rs34221241 [ dbSNP | Ensembl ].
VAR_042062
Natural variant3781R → C in a renal clear cell carcinoma sample; somatic mutation. Ref.39
VAR_042063
Natural variant4941T → A. Ref.38 Ref.39
Corresponds to variant rs307826 [ dbSNP | Ensembl ].
VAR_018407
Natural variant5271N → S. Ref.39
Corresponds to variant rs35874891 [ dbSNP | Ensembl ].
VAR_034379
Natural variant6411P → S. Ref.37 Ref.39
Corresponds to variant rs55667289 [ dbSNP | Ensembl ].
VAR_018408
Natural variant8571G → R in LMPH1A; loss of kinase activity. Ref.19 Ref.37
VAR_018409
Natural variant8681H → Y. Ref.39
Corresponds to variant rs35171798 [ dbSNP | Ensembl ].
VAR_042064
Natural variant8901H → Q. Ref.4 Ref.7 Ref.8 Ref.38
Corresponds to variant rs448012 [ dbSNP | Ensembl ].
VAR_018410
Natural variant9541P → S in HCI. Ref.38
Corresponds to variant rs34255532 [ dbSNP | Ensembl ].
VAR_018411
Natural variant10101T → I in a metastatic melanoma sample; somatic mutation. Ref.39
VAR_042065
Natural variant10311R → Q. Ref.39
Corresponds to variant rs56082504 [ dbSNP | Ensembl ].
VAR_042066
Natural variant10351H → R in LMPH1A; loss of kinase activity. Ref.36
VAR_018412
Natural variant10411R → P in LMPH1A; loss of kinase activity. Ref.17 Ref.37
VAR_018413
Natural variant10441L → P in LMPH1A; loss of kinase activity. Ref.37
VAR_018414
Natural variant10491D → N. Ref.39
Corresponds to variant rs56310180 [ dbSNP | Ensembl ].
VAR_042067
Natural variant10751R → Q. Ref.39
VAR_042068
Natural variant11141P → L in LMPH1A; loss of kinase activity. Ref.35 Ref.37
VAR_018415
Natural variant11371P → S in HCI. Ref.38
VAR_018416
Natural variant11461R → H. Ref.4 Ref.7 Ref.38 Ref.39
Corresponds to variant rs1130379 [ dbSNP | Ensembl ].
VAR_018417

Experimental info

Mutagenesis8791K → G: Abolishes enzyme activity. Ref.17
Mutagenesis10631Y → F: Loss of phosphorylation site. No effect on stimulation of cell proliferation and cell migration. Ref.20 Ref.27
Mutagenesis10681Y → F: Global loss of autophosphorylation. Abolishes stimulation of cell proliferation and cell migration. Ref.20 Ref.27
Mutagenesis12301Y → F: Loss of phosphorylation site. Strongly reduces stimulation of cell proliferation and cell migration. Ref.17 Ref.20
Mutagenesis12311Y → F: Loss of phosphorylation site. Strongly reduces stimulation of cell proliferation and cell migration. Ref.17 Ref.20
Mutagenesis12651Y → F: Loss of phosphorylation site. No effect on stimulation of cell proliferation and cell migration. Ref.17
Mutagenesis13331Y → F: Loss of phosphorylation site. Reduced autophosphorylation. Ref.14 Ref.17
Mutagenesis13371Y → F: Reduced autophosphorylation. Strongly reduces stimulation of cell proliferation and cell migration. Ref.14 Ref.17 Ref.27
Mutagenesis13631Y → F: Loss of phosphorylation site. Slighly reduced autophosphorylation. Ref.14 Ref.17
Sequence conflict241G → D in CAA49505. Ref.3
Sequence conflict241G → D in AAO89504. Ref.7
Sequence conflict241G → D in AAO89505. Ref.7
Sequence conflict5381N → D in BAF84368. Ref.8
Sequence conflict7451R → P in CAA49505. Ref.3
Sequence conflict7451R → P in AAO89504. Ref.7
Sequence conflict7451R → P in AAO89505. Ref.7
Sequence conflict752 – 7532NA → RP in CAA49505. Ref.3
Sequence conflict752 – 7532NA → RP in AAO89504. Ref.7
Sequence conflict752 – 7532NA → RP in AAO89505. Ref.7
Sequence conflict11281L → V in CAA49505. Ref.3
Sequence conflict11281L → V in AAO89504. Ref.7
Sequence conflict11281L → V in AAO89505. Ref.7
Sequence conflict11641E → D in CAA49505. Ref.3

Secondary structure

.............................. 1363
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified November 16, 2011. Version 3.
Checksum: B1473AAAC95E7E93

FASTA1,363152,757
        10         20         30         40         50         60 
MQRGAALCLR LWLCLGLLDG LVSGYSMTPP TLNITEESHV IDTGDSLSIS CRGQHPLEWA 

        70         80         90        100        110        120 
WPGAQEAPAT GDKDSEDTGV VRDCEGTDAR PYCKVLLLHE VHANDTGSYV CYYKYIKARI 

       130        140        150        160        170        180 
EGTTAASSYV FVRDFEQPFI NKPDTLLVNR KDAMWVPCLV SIPGLNVTLR SQSSVLWPDG 

       190        200        210        220        230        240 
QEVVWDDRRG MLVSTPLLHD ALYLQCETTW GDQDFLSNPF LVHITGNELY DIQLLPRKSL 

       250        260        270        280        290        300 
ELLVGEKLVL NCTVWAEFNS GVTFDWDYPG KQAERGKWVP ERRSQQTHTE LSSILTIHNV 

       310        320        330        340        350        360 
SQHDLGSYVC KANNGIQRFR ESTEVIVHEN PFISVEWLKG PILEATAGDE LVKLPVKLAA 

       370        380        390        400        410        420 
YPPPEFQWYK DGKALSGRHS PHALVLKEVT EASTGTYTLA LWNSAAGLRR NISLELVVNV 

       430        440        450        460        470        480 
PPQIHEKEAS SPSIYSRHSR QALTCTAYGV PLPLSIQWHW RPWTPCKMFA QRSLRRRQQQ 

       490        500        510        520        530        540 
DLMPQCRDWR AVTTQDAVNP IESLDTWTEF VEGKNKTVSK LVIQNANVSA MYKCVVSNKV 

       550        560        570        580        590        600 
GQDERLIYFY VTTIPDGFTI ESKPSEELLE GQPVLLSCQA DSYKYEHLRW YRLNLSTLHD 

       610        620        630        640        650        660 
AHGNPLLLDC KNVHLFATPL AASLEEVAPG ARHATLSLSI PRVAPEHEGH YVCEVQDRRS 

       670        680        690        700        710        720 
HDKHCHKKYL SVQALEAPRL TQNLTDLLVN VSDSLEMQCL VAGAHAPSIV WYKDERLLEE 

       730        740        750        760        770        780 
KSGVDLADSN QKLSIQRVRE EDAGRYLCSV CNAKGCVNSS ASVAVEGSED KGSMEIVILV 

       790        800        810        820        830        840 
GTGVIAVFFW VLLLLIFCNM RRPAHADIKT GYLSIIMDPG EVPLEEQCEY LSYDASQWEF 

       850        860        870        880        890        900 
PRERLHLGRV LGYGAFGKVV EASAFGIHKG SSCDTVAVKM LKEGATASEH RALMSELKIL 

       910        920        930        940        950        960 
IHIGNHLNVV NLLGACTKPQ GPLMVIVEFC KYGNLSNFLR AKRDAFSPCA EKSPEQRGRF 

       970        980        990       1000       1010       1020 
RAMVELARLD RRRPGSSDRV LFARFSKTEG GARRASPDQE AEDLWLSPLT MEDLVCYSFQ 

      1030       1040       1050       1060       1070       1080 
VARGMEFLAS RKCIHRDLAA RNILLSESDV VKICDFGLAR DIYKDPDYVR KGSARLPLKW 

      1090       1100       1110       1120       1130       1140 
MAPESIFDKV YTTQSDVWSF GVLLWEIFSL GASPYPGVQI NEEFCQRLRD GTRMRAPELA 

      1150       1160       1170       1180       1190       1200 
TPAIRRIMLN CWSGDPKARP AFSELVEILG DLLQGRGLQE EEEVCMAPRS SQSSEEGSFS 

      1210       1220       1230       1240       1250       1260 
QVSTMALHIA QADAEDSPPS LQRHSLAARY YNWVSFPGCL ARGAETRGSS RMKTFEEFPM 

      1270       1280       1290       1300       1310       1320 
TPTTYKGSVD NQTDSGMVLA SEEFEQIESR HRQESGFSCK GPGQNVAVTR AHPDSQGRRR 

      1330       1340       1350       1360 
RPERGARGGQ VFYNSEYGEL SEPSEEDHCS PSARVTFFTD NSY 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 3DC469ED3CB8B3B1
Show »

FASTA1,298145,599
Isoform 3 (sVegfr3) [UniParc].

Checksum: 873CB1459C93C49A
Show »

FASTA83093,174

References

« Hide 'large scale' references
[1]"FLT4 receptor tyrosine kinase contains seven immunoglobulin-like loops and is expressed in multiple human tissues and cell lines."
Pajusola K., Aprelikova O., Korhonen J., Kaipainen A., Pertovaara L., Alitalo R., Alitalo K.
Cancer Res. 52:5738-5743(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]Erratum
Pajusola K., Aprelikova O., Korhonen J., Kaipainen A., Pertovaara L., Alitalo R., Alitalo K.
Cancer Res. 53:3845-3845(1993)
[3]"Chromosomal localization of FLT4, a novel receptor-type tyrosine kinase gene."
Galland F., Karamysheva A., Mattei M.-G., Rosnet O., Marchetto S., Birnbaum D.
Genomics 13:475-478(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"The FLT4 gene encodes a transmembrane tyrosine kinase related to the vascular endothelial growth factor receptor."
Galland F., Karamysheva A., Pebusque M.-J., Borg J.-P., Rottapel R., Dubreuil P., Rosnet O., Birnbaum D.
Oncogene 8:1233-1240(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLN-890 AND HIS-1146.
Tissue: Placenta.
[5]"Vascular endothelial growth factor-related protein: a ligand and specific activator of the tyrosine kinase receptor Flt4."
Lee J., Gray A., Yuan J., Luoh S.-M., Avraham H., Wood W.I.
Proc. Natl. Acad. Sci. U.S.A. 93:1988-1992(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH VEGFC, PHOSPHORYLATION, FUNCTION IN CELL PROLIFERATION.
[6]"Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH VEGFD, SUBCELLULAR LOCATION.
[7]Lian Z., Feitelson M.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS GLN-890 AND HIS-1146.
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLN-890.
Tissue: Placenta.
[9]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"FLT4, a novel class III receptor tyrosine kinase in chromosome 5q33-qter."
Aprelikova O., Pajusola K., Partanen J., Armstrong E., Alitalo R., Bailey S.K., McMahon J., Wasmuth J., Huebner K., Alitalo K.
Cancer Res. 52:746-748(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 761-1190.
[11]"Two human FLT4 receptor tyrosine kinase isoforms with distinct carboxy terminal tails are produced by alternative processing of primary transcripts."
Pajusola K., Aprelikova O., Armstrong E., Morris S., Alitalo K.
Oncogene 8:2931-2937(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1293-1363 (ISOFORM 1), ALTERNATIVE SPLICING.
[12]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-39.
[13]"Biochemical characterization of two isoforms of FLT4, a VEGF receptor-related tyrosine kinase."
Borg J.P., deLapeyriere O., Noguchi T., Rottapel R., Dubreuil P., Birnbaum D.
Oncogene 10:973-984(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
[14]"Mutation at tyrosine residue 1337 abrogates ligand-dependent transforming capacity of the FLT4 receptor."
Fournier E., Dubreuil P., Birnbaum D., Borg J.P.
Oncogene 11:921-931(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION AND PHOSPHORYLATION OF SHC1, CHARACTERIZATION OF ISOFORM 1 AND ISOFORM 2, INTERACTION WITH SHC1 AND GRB2, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-1333; TYR-1337 AND TYR-1363, TISSUE SPECIFICITY.
[15]"Vascular endothelial growth factor D (VEGF-D) is a ligand for the tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4)."
Achen M.G., Jeltsch M., Kukk E., Maekinen T., Vitali A., Wilks A.F., Alitalo K., Stacker S.A.
Proc. Natl. Acad. Sci. U.S.A. 95:548-553(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VEGFD, FUNCTION AS VEGFD RECEPTOR, AUTOPHOSPHORYLATION.
[16]"Isolated lymphatic endothelial cells transduce growth, survival and migratory signals via the VEGF-C/D receptor VEGFR-3."
Makinen T., Veikkola T., Mustjoki S., Karpanen T., Catimel B., Nice E.C., Wise L., Mercer A., Kowalski H., Kerjaschki D., Stacker S.A., Achen M.G., Alitalo K.
EMBO J. 20:4762-4773(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RECEPTOR FOR VEGFC AND VEGFD IN CELL SURVIVAL; PROLIFERATION AND MIGRATION, FUNCTION IN ACTIVATION OF PROTEIN KINASE C; AKT1; PIK3R1; MAPK1/ERK2 AND MAPK3/ERK1.
[17]"Ligand-induced vascular endothelial growth factor receptor-3 (VEGFR-3) heterodimerization with VEGFR-2 in primary lymphatic endothelial cells regulates tyrosine phosphorylation sites."
Dixelius J., Makinen T., Wirzenius M., Karkkainen M.J., Wernstedt C., Alitalo K., Claesson-Welsh L.
J. Biol. Chem. 278:40973-40979(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, CHARACTERIZATION OF VARIANT LMPH1A PRO-1041, MUTAGENESIS OF LYS-879; TYR-1230; TYR-1231; TYR-1265; TYR-1333; TYR-1337 AND TYR-1363, PHOSPHORYLATION AT TYR-1230; TYR-1231; TYR-1265; TYR-1333; TYR-1337 AND TYR-1363.
[18]"Heterodimerization with vascular endothelial growth factor receptor-2 (VEGFR-2) is necessary for VEGFR-3 activity."
Alam A., Herault J.P., Barron P., Favier B., Fons P., Delesque-Touchard N., Senegas I., Laboudie P., Bonnin J., Cassan C., Savi P., Ruggeri B., Carmeliet P., Bono F., Herbert J.M.
Biochem. Biophys. Res. Commun. 324:909-915(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN KDR SIGNALING AND IN ANGIOGENESIS, INTERACTION WITH KDR, PHOSPHORYLATION.
[19]"Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
Wang J.F., Zhang X., Groopman J.E.
J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL SURVIVAL, PHOSPHORYLATION IN RESPONSE TO OXIDATIVE STRESS, INTERACTION WITH PIK3R1; SHC1; GRB2; PTPN11 AND PLCG1, ENZYME REGULATION BY MAZ51, CHARACTERIZATION OF VARIANT LMPH1A ARG-857.
[20]"Direct recruitment of CRK and GRB2 to VEGFR-3 induces proliferation, migration, and survival of endothelial cells through the activation of ERK, AKT, and JNK pathways."
Salameh A., Galvagni F., Bardelli M., Bussolino F., Oliviero S.
Blood 106:3423-3431(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF AKT1; MAPK1/ERK2; MAPK3/ERK1 AND MAPK8, FUNCTION IN PROMOTING CELL SURVIVAL; PROLIFERATION AND MIGRATION, CHARACTERIZATION OF ISOFORM 1 AND ISOFORM 2, INTERACTION WITH CRK AND GRB2, PHOSPHORYLATION AT TYR-1063; TYR-1068; TYR-1230; TYR-1231 AND TYR-1337, MUTAGENESIS OF TYR-1063; TYR-1068; TYR-1230 AND TYR-1231.
[21]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-527.
Tissue: Plasma.
[22]"Vascular endothelial growth factor receptor-3 and focal adhesion kinase bind and suppress apoptosis in breast cancer cells."
Garces C.A., Kurenova E.V., Golubovskaya V.M., Cance W.G.
Cancer Res. 66:1446-1454(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROMOTING CELL SURVIVAL, INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION.
[23]"Cooperative and redundant roles of VEGFR-2 and VEGFR-3 signaling in adult lymphangiogenesis."
Goldman J., Rutkowski J.M., Shields J.D., Pasquier M.C., Cui Y., Schmokel H.G., Willey S., Hicklin D.J., Pytowski B., Swartz M.A.
FASEB J. 21:1003-1012(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LYMPHANGIOGENESIS.
[24]"Autocrine loop between vascular endothelial growth factor (VEGF)-C and VEGF receptor-3 positively regulates tumor-associated lymphangiogenesis in oral squamoid cancer cells."
Matsuura M., Onimaru M., Yonemitsu Y., Suzuki H., Nakano T., Ishibashi H., Shirasuna K., Sueishi K.
Am. J. Pathol. 175:1709-1721(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN CANCER, FUNCTION AS VEGFC RECEPTOR IN TUMOR LYMPHANGIOGENESIS; CELL PROLIFERATION; CELL SURVIVAL; IN ACTIVATION OF PIK3R1; AKT1 AND MAP KINASES AND IN UP-REGULATION OF VEGFA AND VEGFC EXPRESSION, ENZYME REGULATION, AUTOPHOSPHORYLATION.
[25]"Small molecule chloropyramine hydrochloride (C4) targets the binding site of focal adhesion kinase and vascular endothelial growth factor receptor 3 and suppresses breast cancer growth in vivo."
Kurenova E.V., Hunt D.L., He D., Magis A.T., Ostrov D.A., Cance W.G.
J. Med. Chem. 52:4716-4724(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN CANCER, INTERACTION WITH PTK2/FAK1.
[26]"Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function and choanal development in humans."
Au A.C., Hernandez P.A., Lieber E., Nadroo A.M., Shen Y.M., Kelley K.A., Gelb B.D., Diaz G.A.
Am. J. Hum. Genet. 87:436-444(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN14.
[27]"Endothelial cell adhesion to the extracellular matrix induces c-Src-dependent VEGFR-3 phosphorylation without the activation of the receptor intrinsic kinase activity."
Galvagni F., Pennacchini S., Salameh A., Rocchigiani M., Neri F., Orlandini M., Petraglia F., Gotta S., Sardone G.L., Matteucci G., Terstappen G.C., Oliviero S.
Circ. Res. 106:1839-1848(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-830; TYR-833; TYR-853; TYR-1063; TYR-1068; TYR-1333 AND TYR-1337, IDENTIFICATION IN A COMPLEX WITH SRC AND ITGB1, MUTAGENESIS OF TYR-1063; TYR-1068 AND TYR-1337, ENZYME REGULATION BY MAZ51, INTERACTION WITH ITGB1; CRK AND SHC1, FUNCTION IN ACTIVATION OF MAPK8 AND IN REGULATION OF ANGIOGENIC SPROUTING, IDENTIFICATION BY MASS SPECTROMETRY.
[28]"VEGF receptor 2/-3 heterodimers detected in situ by proximity ligation on angiogenic sprouts."
Nilsson I., Bahram F., Li X., Gualandi L., Koch S., Jarvius M., Soderberg O., Anisimov A., Kholova I., Pytowski B., Baldwin M., Yla-Herttuala S., Alitalo K., Kreuger J., Claesson-Welsh L.
EMBO J. 29:1377-1388(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KDR, FUNCTION IN MODULATING KDR SIGNALING AND IN ANGIOGENESIS, TISSUE SPECIFICITY.
[29]"Ephrin-B2 controls VEGF-induced angiogenesis and lymphangiogenesis."
Wang Y., Nakayama M., Pitulescu M.E., Schmidt T.S., Bochenek M.L., Sakakibara A., Adams S., Davy A., Deutsch U., Luthi U., Barberis A., Benjamin L.E., Makinen T., Nobes C.D., Adams R.H.
Nature 465:483-486(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS, SUBCELLULAR LOCATION.
[30]"Combined blockade of VEGFR-2 and VEGFR-3 inhibits inflammatory lymphangiogenesis in early and middle stages."
Yuen D., Pytowski B., Chen L.
Invest. Ophthalmol. Vis. Sci. 52:2593-2597(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LYMPHANGIOGENESIS.
[31]"VEGF receptor protein-tyrosine kinases: structure and regulation."
Roskoski R. Jr.
Biochem. Biophys. Res. Commun. 375:287-291(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON STRUCTURE AND FUNCTION.
[32]"VEGFs and receptors involved in angiogenesis versus lymphangiogenesis."
Lohela M., Bry M., Tammela T., Alitalo K.
Curr. Opin. Cell Biol. 21:154-165(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN LYMPHANGIOGENESIS AND CANCER.
[33]"Signal transduction by vascular endothelial growth factor receptors."
Koch S., Tugues S., Li X., Gualandi L., Claesson-Welsh L.
Biochem. J. 437:169-183(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON LIGAND SPECIFICITY; FUNCTION; STRUCTURE; PHOSPHORYLATION AND SIGNALING.
[34]"Lymphangiogenesis and cancer metastasis."
Al-Rawi M.A., Jiang W.G.
Front. Biosci. 16:723-739(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN LYMPHANGIOGENESIS AND ROLE IN CANCER.
[35]"Hereditary lymphedema: evidence for linkage and genetic heterogeneity."
Ferrell R.E., Levinson K.L., Esman J.H., Kimak M.A., Lawrence E.C., Barmada M.M., Finegold D.N.
Hum. Mol. Genet. 7:2073-2078(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LMPH1A LEU-1114.
[36]"Congenital hereditary lymphedema caused by a mutation that inactivates VEGFR3 tyrosine kinase."
Irrthum A., Karkkainen M.J., Devriendt K., Alitalo K., Vikkula M.
Am. J. Hum. Genet. 67:295-301(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LMPH1A, CHARACTERIZATION OF VARIANT LMPH1A ARG-1035.
[37]"Missense mutations interfere with VEGFR-3 signalling in primary lymphoedema."
Karkkainen M.J., Ferrell R.E., Lawrence E.C., Kimak M.A., Levinson K.L., McTigue M.A., Alitalo K., Finegold D.N.
Nat. Genet. 25:153-159(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LMPH1A ARG-857; PRO-1041; PRO-1044 AND LEU-1114, VARIANT SER-641, CHARACTERIZATION OF VARIANTS.
[38]"Somatic mutation of vascular endothelial growth factor receptors in juvenile hemangioma."
Walter J.W., North P.E., Waner M., Mizeracki A., Blei F., Walker J.W.T., Reinisch J.F., Marchuk D.A.
Genes Chromosomes Cancer 33:295-303(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HCI SER-954 AND SER-1137, VARIANTS ALA-494; GLN-890 AND HIS-1146.
[39]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-149; CYS-378; ALA-494; SER-527; SER-641; TYR-868; ILE-1010; GLN-1031; ASN-1049; GLN-1075 AND HIS-1146.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69878 mRNA. Translation: CAA49505.1.
U43143 mRNA. Translation: AAA85215.1.
EU826564 mRNA. Translation: ACF47600.1.
AY233382 mRNA. Translation: AAO89504.1.
AY233383 mRNA. Translation: AAO89505.1.
AK291679 mRNA. Translation: BAF84368.1.
AC122714 Genomic DNA. No translation available.
X68203 mRNA. Translation: CAA48290.1. Different initiation.
S66407 mRNA. Translation: AAB28539.1.
PIRA48999.
RefSeqNP_002011.2. NM_002020.4.
NP_891555.2. NM_182925.4.
UniGeneHs.646917.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BSJX-ray2.50A328-553[»]
4BSKX-ray4.20A23-229[»]
ProteinModelPortalP35916.
SMRP35916. Positions 28-553, 632-765, 823-1180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108612. 9 interactions.
DIPDIP-5739N.
IntActP35916. 5 interactions.
MINTMINT-1182429.
STRING9606.ENSP00000261937.

Chemistry

BindingDBP35916.
ChEMBLCHEMBL1955.
DrugBankDB00398. Sorafenib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGY1814.

PTM databases

PhosphoSiteP35916.

Polymorphism databases

DMDM357529070.

Proteomic databases

PaxDbP35916.
PRIDEP35916.

Protocols and materials databases

DNASU2324.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261937; ENSP00000261937; ENSG00000037280. [P35916-2]
ENST00000393347; ENSP00000377016; ENSG00000037280. [P35916-1]
GeneID2324.
KEGGhsa:2324.
UCSCuc003mlz.4. human. [P35916-2]
uc003mma.4. human. [P35916-1]
uc011dgy.2. human. [P35916-3]

Organism-specific databases

CTD2324.
GeneCardsGC05M180028.
HGNCHGNC:3767. FLT4.
HPACAB000099.
MIM136352. gene.
153100. phenotype.
602089. phenotype.
neXtProtNX_P35916.
Orphanet79452. Milroy disease.
PharmGKBPA28183.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000037949.
HOVERGENHBG053432.
KOK05097.
OMAQINEEFC.
OrthoDBEOG75F4CC.
PhylomeDBP35916.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkP35916.

Gene expression databases

ArrayExpressP35916.
BgeeP35916.
CleanExHS_FLT4.
GenevestigatorP35916.

Family and domain databases

Gene3D2.60.40.10. 9 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
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.
IPR009137. VEGFR3_rcpt.
[Graphical view]
PANTHERPTHR24416:SF49. PTHR24416:SF49. 1 hit.
PfamPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR01835. VEGFRECEPTR3.
SMARTSM00409. IG. 4 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. 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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFLT4. human.
GeneWikiFLT4.
GenomeRNAi2324.
NextBio9433.
PROP35916.
SOURCESearch...

Entry information

Entry nameVGFR3_HUMAN
AccessionPrimary (citable) accession number: P35916
Secondary accession number(s): A8K6L4 expand/collapse secondary AC list , B5A926, Q16067, Q86W07, Q86W08
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 16, 2011
Last modified: April 16, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM