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P35969

- VGFR1_MOUSE

UniProt

P35969 - VGFR1_MOUSE

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Protein
Vascular endothelial growth factor receptor 1
Gene
Flt1, Emrk2, Flt, Vegfr1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, and proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts. Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to the activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC, YES1 and PLCG, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 and PTK2/FAK1 By similarity.6 Publications

Catalytic activityi

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

Enzyme regulationi

Present in an inactive conformation in the absence of bound ligand. Binding of VEGFA, VEGFB or PGF leads to dimerization and activation by autophosphorylation on tyrosine residues By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei768 – 7692Cleavage; by PSEN1 By similarity
Binding sitei862 – 8621ATP By similarity
Active sitei1022 – 10221Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi834 – 8429ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. VEGF-A-activated receptor activity Source: Ensembl
  3. VEGF-B-activated receptor activity Source: Ensembl
  4. identical protein binding Source: MGI
  5. placental growth factor-activated receptor activity Source: Ensembl
  6. vascular endothelial growth factor-activated receptor activity Source: MGI

GO - Biological processi

  1. angiogenesis Source: UniProtKB
  2. blood vessel morphogenesis Source: UniProtKB
  3. cell differentiation Source: UniProtKB-KW
  4. cell migration Source: UniProtKB
  5. embryonic morphogenesis Source: UniProtKB
  6. monocyte chemotaxis Source: Ensembl
  7. patterning of blood vessels Source: MGI
  8. peptidyl-tyrosine phosphorylation Source: UniProtKB
  9. positive regulation of MAP kinase activity Source: Ensembl
  10. positive regulation of angiogenesis Source: Ensembl
  11. positive regulation of cell migration Source: Ensembl
  12. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
  13. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  14. positive regulation of phospholipase C activity Source: Ensembl
  15. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: Ensembl
  16. protein autophosphorylation Source: UniProtKB
  17. sprouting angiogenesis Source: MGI
  18. vascular endothelial growth factor receptor signaling pathway Source: MGI
  19. vascular endothelial growth factor signaling pathway Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Angiogenesis, Chemotaxis, Differentiation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_205099. VEGF binds to VEGFR leading to receptor dimerization.
REACT_227870. Neurophilin interactions with VEGF and VEGFR.

Names & Taxonomyi

Protein namesi
Recommended name:
Vascular endothelial growth factor receptor 1 (EC:2.7.10.1)
Short name:
VEGFR-1
Alternative name(s):
Embryonic receptor kinase 2
Fms-like tyrosine kinase 1
Short name:
FLT-1
Tyrosine-protein kinase receptor FLT
Gene namesi
Name:Flt1
Synonyms:Emrk2, Flt, Vegfr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:95558. Flt1.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Endosome By similarity
Note: Autophosphorylation promotes ubiquitination and endocytosis By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 759737Extracellular Reviewed prediction
Add
BLAST
Transmembranei760 – 78122Helical; Reviewed prediction
Add
BLAST
Topological domaini782 – 1333552Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. endosome Source: UniProtKB-SubCell
  3. integral component of plasma membrane Source: UniProtKB
  4. nucleus Source: Ensembl
  5. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane

Pathology & Biotechi

Disruption phenotypei

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 13331311Vascular endothelial growth factor receptor 1
PRO_0000016769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi53 ↔ 108 By similarity
Glycosylationi101 – 1011N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi159 ↔ 208 By similarity
Glycosylationi165 – 1651N-linked (GlcNAc...) Reviewed prediction
Glycosylationi197 – 1971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi252 – 2521N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi253 ↔ 312 By similarity
Glycosylationi324 – 3241N-linked (GlcNAc...) Reviewed prediction
Glycosylationi418 – 4181N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi455 ↔ 536 By similarity
Glycosylationi475 – 4751N-linked (GlcNAc...) Reviewed prediction
Glycosylationi517 – 5171N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi578 ↔ 637 By similarity
Glycosylationi598 – 5981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi626 – 6261N-linked (GlcNAc...) Reviewed prediction
Glycosylationi667 – 6671N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi683 ↔ 732 By similarity
Glycosylationi714 – 7141N-linked (GlcNAc...) Reviewed prediction
Modified residuei915 – 9151Phosphotyrosine; by autocatalysis By similarity
Modified residuei1053 – 10531Phosphotyrosine; by autocatalysis By similarity
Modified residuei1169 – 11691Phosphotyrosine; by autocatalysis By similarity
Modified residuei1213 – 12131Phosphotyrosine; by autocatalysis By similarity
Modified residuei1242 – 12421Phosphotyrosine; by autocatalysis By similarity
Modified residuei1322 – 13221Phosphotyrosine; by autocatalysis By similarity
Modified residuei1328 – 13281Phosphotyrosine; by autocatalysis By similarity

Post-translational modificationi

N-glycosylated By similarity.
Ubiquitinated after VEGFA-mediated autophosphorylation, leading to proteolytic degradation By similarity.
Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-1169 is important for interaction with PLCG. Phosphorylation at Tyr-1213 is important for interaction with PIK3R1, PTPN11, GRB2, and PLCG. Phosphorylation at Tyr-1328 is important for endocytosis and for interaction with CBL, NCK1 and CRK. Is probably dephosphorylated by PTPRB By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP35969.
PRIDEiP35969.

PTM databases

PhosphoSiteiP35969.

Expressioni

Gene expression databases

ArrayExpressiP35969.
BgeeiP35969.
CleanExiMM_FLT1.
GenevestigatoriP35969.

Interactioni

Subunit structurei

Interacts with VEGFA, VEGFB and PGF. Monomer in the absence of bound VEGFA, VEGFB or PGF. Homodimer in the presence of bound VEGFA, VEGFB and PGF. Can also form a heterodimer with KDR. Interacts (tyrosine phosphorylated) with CBL, CRK, GRB2, NCK1, PIK3R1, PLCG, PSEN1 and PTPN11. Probably interacts with PTPRB. Interacts with GNB2L1/RACK1. Identified in a complex with CBL and CD2AP By similarity.

Protein-protein interaction databases

BioGridi199706. 5 interactions.
DIPiDIP-39359N.
IntActiP35969. 8 interactions.
MINTiMINT-4139959.

Structurei

3D structure databases

ProteinModelPortaliP35969.
SMRiP35969. Positions 32-751, 788-1197.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 12493Ig-like C2-type 1
Add
BLAST
Domaini152 – 21564Ig-like C2-type 2
Add
BLAST
Domaini231 – 32898Ig-like C2-type 3
Add
BLAST
Domaini334 – 42996Ig-like C2-type 4
Add
BLAST
Domaini430 – 550121Ig-like C2-type 5
Add
BLAST
Domaini557 – 656100Ig-like C2-type 6
Add
BLAST
Domaini662 – 74887Ig-like C2-type 7
Add
BLAST
Domaini828 – 1158331Protein kinase
Add
BLAST

Domaini

The second and third Ig-like C2-type (immunoglobulin-like) domains are sufficient for VEGFA binding By similarity.

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00720000108679.
HOGENOMiHOG000037949.
HOVERGENiHBG053432.
InParanoidiP35969.
KOiK05096.
OrthoDBiEOG75F4CC.
PhylomeDBiP35969.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
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.
IPR009135. VEGFR1_rcpt.
[Graphical view]
PANTHERiPTHR24416:SF126. PTHR24416:SF126. 1 hit.
PfamiPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01833. VEGFRECEPTR1.
SMARTiSM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35969-1 [UniParc]FASTAAdd to Basket

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MVSCWDTAVL PYALLGCLLL TGYGSGSKLK VPELSLKGTQ HVMQAGQTLF     50
LKCRGEAAHS WSLPTTVSQE DKRLSITPPS ACGRDNRQFC STLTLDTAQA 100
NHTGLYTCRY LPTSTSKKKK AESSIYIFVS DAGSPFIEMH TDIPKLVHMT 150
EGRQLIIPCR VTSPNVTVTL KKFPFDTLTP DGQRITWDSR RGFIIANATY 200
KEIGLLNCEA TVNGHLYQTN YLTHRQTNTI LDVQIRPPSP VRLLHGQTLV 250
LNCTATTELN TRVQMSWNYP GKATKRASIR QRIDRSHSHN NVFHSVLKIN 300
NVESRDKGLY TCRVKSGSSF QSFNTSVHVY EKGFISVKHR KQPVQETTAG 350
RRSYRLSMKV KAFPSPEIVW LKDGSPATLK SARYLVHGYS LIIKDVTTED 400
AGDYTILLGI KQSRLFKNLT ATLIVNVKPQ IYEKSVSSLP SPPLYPLGSR 450
QVLTCTVYGI PRPTITWLWH PCHHNHSKER YDFCTENEES FILDPSSNLG 500
NRIESISQRM TVIEGTNKTV STLVVADSQT PGIYSCRAFN KIGTVERNIK 550
FYVTDVPNGF HVSLEKMPAE GEDLKLSCVV NKFLYRDITW ILLRTVNNRT 600
MHHSISKQKM ATTQDYSITL NLVIKNVSLE DSGTYACRAR NIYTGEDILR 650
KTEVLVRDSE APHLLQNLSD YEVSISGSTT LDCQARGVPA PQITWFKNNH 700
KIQQEPGIIL GPGNSTLFIE RVTEEDEGVY RCRATNQKGA VESAAYLTVQ 750
GTSDKSNLEL ITLTCTCVAA TLFWLLLTLF IRKLKRSSSE VKTDYLSIIM 800
DPDEVPLDEQ CERLPYDASK WEFARERLKL GKSLGRGAFG KVVQASAFGI 850
KKSPTCRTVA VKMLKEGATA SEYKALMTEL KILTHIGHHL NVVNLLGACT 900
KQGGPLMVIV EYCKYGNLSN YLKSKRDLFC LNKDAALHME LKKESLEPGL 950
EQGQKPRLDS VSSSSVTSSS FPEDRSVSDV EGDEDYSEIS KQPLTMEDLI 1000
SYSFQVARGM EFLSSRKCIH RDLAARNILL SENNVVKICD FGLARDIYKN 1050
PDYVRRGDTR LPLKWMAPES IFDKVYSTKS DVWSYGVLLW EIFSLGGSPY 1100
PGVQMDEDFC SRLKEGMRMR TPEYATPEIY QIMLDCWHKD PKERPRFAEL 1150
VEKLGDLLQA NVQQDGKDYI PLNAILTRNS SFTYSTPTFS EDLFKDGFAD 1200
PHFHSGSSDD VRYVNAFKFM SLERIKTFEE LSPNSTSMFE DYQLDTSTLL 1250
GSPLLKRFTW TETKPKASMK IDLRIASKSK EAGLSDLPRP SFCFSSCGHI 1300
RPVQDDESEL GKESCCSPPP DYNSVVLYSS PPA 1333
Length:1,333
Mass (Da):149,876
Last modified:June 1, 1994 - v1
Checksum:iC06533B7ECBC404C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581Missing in CAA55311. 1 Publication
Sequence conflicti211 – 2111Missing in CAA55311. 1 Publication
Sequence conflicti245 – 2451H → L in CAA55311. 1 Publication
Sequence conflicti603 – 6031H → N in CAA55311. 1 Publication
Sequence conflicti609 – 6157KMATTQD → NGHHSS in CAA55311. 1 Publication
Sequence conflicti696 – 6961F → L in CAA55311. 1 Publication
Sequence conflicti734 – 7341A → S in CAA55311. 1 Publication
Sequence conflicti765 – 7651C → Y in CAA55311. 1 Publication
Sequence conflicti820 – 8201K → N in CAA55311. 1 Publication
Sequence conflicti1009 – 10091G → R in CAA55311. 1 Publication
Sequence conflicti1181 – 11811S → G in BAA24498. 1 Publication
Sequence conflicti1181 – 11811S → N in CAA55311. 1 Publication
Sequence conflicti1193 – 11942LF → RG in CAA55311. 1 Publication
Sequence conflicti1278 – 12792KS → PR in CAA55311. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07297 mRNA. Translation: AAA40078.1.
X78568 mRNA. Translation: CAA55311.1.
D88689 mRNA. Translation: BAA24498.1.
CCDSiCCDS19879.1.
PIRiI78875.
S49010.
RefSeqiNP_034358.2. NM_010228.3.
UniGeneiMm.389712.

Genome annotation databases

EnsembliENSMUST00000031653; ENSMUSP00000031653; ENSMUSG00000029648.
GeneIDi14254.
KEGGimmu:14254.
UCSCiuc009aoh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07297 mRNA. Translation: AAA40078.1 .
X78568 mRNA. Translation: CAA55311.1 .
D88689 mRNA. Translation: BAA24498.1 .
CCDSi CCDS19879.1.
PIRi I78875.
S49010.
RefSeqi NP_034358.2. NM_010228.3.
UniGenei Mm.389712.

3D structure databases

ProteinModelPortali P35969.
SMRi P35969. Positions 32-751, 788-1197.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199706. 5 interactions.
DIPi DIP-39359N.
IntActi P35969. 8 interactions.
MINTi MINT-4139959.

Chemistry

BindingDBi P35969.
ChEMBLi CHEMBL3516.

PTM databases

PhosphoSitei P35969.

Proteomic databases

PaxDbi P35969.
PRIDEi P35969.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031653 ; ENSMUSP00000031653 ; ENSMUSG00000029648 .
GeneIDi 14254.
KEGGi mmu:14254.
UCSCi uc009aoh.1. mouse.

Organism-specific databases

CTDi 2321.
MGIi MGI:95558. Flt1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00720000108679.
HOGENOMi HOG000037949.
HOVERGENi HBG053432.
InParanoidi P35969.
KOi K05096.
OrthoDBi EOG75F4CC.
PhylomeDBi P35969.
TreeFami TF325768.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 3474.
Reactomei REACT_205099. VEGF binds to VEGFR leading to receptor dimerization.
REACT_227870. Neurophilin interactions with VEGF and VEGFR.

Miscellaneous databases

ChiTaRSi FLT1. mouse.
NextBioi 285579.
PROi P35969.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35969.
Bgeei P35969.
CleanExi MM_FLT1.
Genevestigatori P35969.

Family and domain databases

Gene3Di 2.60.40.10. 7 hits.
InterProi IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013106. Ig_V-set.
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.
IPR009135. VEGFR1_rcpt.
[Graphical view ]
PANTHERi PTHR24416:SF126. PTHR24416:SF126. 1 hit.
Pfami PF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view ]
PRINTSi PR01833. VEGFRECEPTR1.
SMARTi SM00409. IG. 5 hits.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS50835. IG_LIKE. 5 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of murine FLT and FLT4."
    Finnerty H., Kelleher K., Morris G.E., Bean K., Merberg D.M., Kriz R., Morris J.C., Sookdeo H., Turner K.J., Wood C.R.
    Oncogene 8:2293-2298(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Neonatal brain and Placenta.
  2. "Isolation of a gene encoding a novel receptor tyrosine kinase from differentiated embryonic stem cells."
    Choi K., Wall C., Hanratty R., Keller G.
    Oncogene 9:1261-1266(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Genomic organization of the flt-1 gene encoding for vascular endothelial growth factor (VEGF) receptor-1 suggests an intimate evolutionary relationship between the 7-Ig and the 5-Ig tyrosine kinase receptors."
    Kondo K., Hiratsuka S., Subbalakshmi E., Matsushime H., Shibuya M.
    Gene 208:297-305(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Lung.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 110-119 AND 185-191, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Role of the Flt-1 receptor tyrosine kinase in regulating the assembly of vascular endothelium."
    Fong G.H., Rossant J., Gertsenstein M., Breitman M.L.
    Nature 376:66-70(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN BLOOD VESSEL DEVELOPMENT DURING EMBRYOGENESIS.
  6. "Flt-1 lacking the tyrosine kinase domain is sufficient for normal development and angiogenesis in mice."
    Hiratsuka S., Minowa O., Kuno J., Noda T., Shibuya M.
    Proc. Natl. Acad. Sci. U.S.A. 95:9349-9354(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN MACROPHAGE MIGRATION.
  7. "Involvement of Flt-1 tyrosine kinase (vascular endothelial growth factor receptor-1) in pathological angiogenesis."
    Hiratsuka S., Maru Y., Okada A., Seiki M., Noda T., Shibuya M.
    Cancer Res. 61:1207-1213(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  8. "The VEGF receptor flt-1 (VEGFR-1) is a positive modulator of vascular sprout formation and branching morphogenesis."
    Kearney J.B., Kappas N.C., Ellerstrom C., DiPaola F.W., Bautch V.L.
    Blood 103:4527-4535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Vascular endothelial growth factor receptor-1 regulates postnatal angiogenesis through inhibition of the excessive activation of Akt."
    Nishi J., Minamino T., Miyauchi H., Nojima A., Tateno K., Okada S., Orimo M., Moriya J., Fong G.H., Sunagawa K., Shibuya M., Komuro I.
    Circ. Res. 103:261-268(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ANGIOGENESIS.
  10. "Vascular endothelial growth factor receptor-1 signaling promotes mobilization of macrophage lineage cells from bone marrow and stimulates solid tumor growth."
    Muramatsu M., Yamamoto S., Osawa T., Shibuya M.
    Cancer Res. 70:8211-8221(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiVGFR1_MOUSE
AccessioniPrimary (citable) accession number: P35969
Secondary accession number(s): O55094, Q61517
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi