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Protein Page:
VEGF (rat)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
VEGF Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Defects in VEGFA are a cause of susceptibility to microvascular complications of diabetes type 1 (MVCD1). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Belongs to the PDGF/VEGF growth factor family. 13 isoforms of the human protein are produced by alternative promoter. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Motility/polarity/chemotaxis; Cytokine; Secreted
Cellular Component: extracellular space; cell surface; membrane; cytoplasm; basement membrane; secretory granule
Molecular Function: heparin binding; identical protein binding; protein homodimerization activity; growth factor activity; vascular endothelial growth factor receptor 2 binding; protein heterodimerization activity; fibronectin binding; platelet-derived growth factor receptor binding; cytokine activity; vascular endothelial growth factor receptor 1 binding; vascular endothelial growth factor receptor binding; receptor agonist activity; chemoattractant activity
Biological Process: heart morphogenesis; macrophage differentiation; positive regulation of positive chemotaxis; positive regulation of cell adhesion; positive regulation of receptor internalization; cell maturation; response to vitamin A; basophil chemotaxis; positive regulation of MAP kinase activity; regulation of cell shape; positive chemotaxis; response to folic acid; positive regulation of mesenchymal cell proliferation; mesoderm development; negative regulation of neuron apoptosis; kidney development; nervous system development; positive regulation of neuroblast proliferation; T-helper 1 type immune response; positive regulation of signal transduction; monocyte differentiation; mRNA stabilization; positive regulation of blood vessel endothelial cell migration; activation of CREB transcription factor; positive regulation of protein amino acid autophosphorylation; positive regulation of vascular permeability; patterning of blood vessels; regulation of transcription from RNA polymerase II promoter; positive regulation of angiogenesis; positive regulation of peptidyl-tyrosine phosphorylation; eye photoreceptor cell development; camera-type eye morphogenesis; branching morphogenesis of a tube; cell migration during sprouting angiogenesis; cardiac muscle fiber development; positive regulation of cell division; positive regulation of axon extension involved in axon guidance; activation of protein kinase activity; neuron development; blood vessel morphogenesis; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; response to progesterone stimulus; alveolus development; surfactant homeostasis; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; lactation; post-embryonic camera-type eye development; positive regulation of smooth muscle cell proliferation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of caspase activity; response to estradiol stimulus; positive regulation of vascular endothelial growth factor receptor signaling pathway; induction of positive chemotaxis; vasculature development; epithelial cell differentiation; positive regulation of focal adhesion formation; ovarian follicle development; positive regulation of cell proliferation; negative regulation of programmed cell death; angiogenesis; negative regulation of bone resorption; cell differentiation; blood vessel development; cell migration; in utero embryonic development; lumen formation; positive regulation of cell motility; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein kinase B signaling cascade; cell proliferation; positive regulation of protein complex assembly; response to hypoxia; artery morphogenesis; blood vessel remodeling; positive regulation of protein amino acid phosphorylation; response to cold; vascular endothelial growth factor receptor signaling pathway; hyaluronan metabolic process; growth; lung development; positive regulation of cell migration
Reference #:  NP_114024 (RefSeq)
Alt. Names/Synonyms: Vascular endothelial growth factor A; Vascular permeability factor; Vegf; VEGF-A; Vegfa; VPF
Gene Symbols: Vegfa
Molecular weight: 43,084 Da
Basal Isoelectric point: 9.41  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis
Select Structure to View Below

VEGF

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  Pfam  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       rat

► Hide Isoforms
 
0 17 K320 DRTKPEKKSVRGkGk
0 253 K325-a EKKSVRGkGkGQkRK
0 254 K327-a KSVRGkGkGQkRKRK
0 254 K330-a RGkGkGQkRKRKKSR
  VEGF iso2  
- gap
- gap
- gap
- gap
  human

► Hide Isoforms
 
K142 DRARQEKKSVRGKGK
K147 EKKSVRGKGKGQKRK
K149 KSVRGKGKGQKRKRK
K152 RGKGKGQKRKRKKSR
  VEGF iso4  
- gap
- gap
- gap
- gap
  VEGF iso6  
K142 DRARQEKKSVRGKGK
K147 EKKSVRGKGKGQKRK
K149 KSVRGKGKGQKRKRK
K152 RGKGKGQKRKRKKSR
  VEGF iso10  
- gap
- gap
- gap
- gap
  VEGF iso14  
K322-a DRARQEKkSVRGkGk
K327-a EKkSVRGkGkGQkRK
K329-a kSVRGkGkGQkRKRK
K332-a RGkGkGQkRKRKKSR
  mouse

 
K319 DRTKPEKKSVRGkGk
K324-a EKKSVRGkGkGQkRK
K326-a KSVRGkGkGQkRKRK
K329-a RGkGkGQkRKRKKSR
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