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Protein Page:
VEGF (mouse)
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

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; Secreted, signal peptide; Cytokine; Motility/polarity/chemotaxis
Cellular Component: extracellular space; cell surface; membrane; cytoplasm; plasma membrane; extracellular region; basement membrane; secretory granule
Molecular Function: heparin binding; identical protein binding; protein homodimerization activity; growth factor activity; extracellular matrix 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; protein binding; vascular endothelial growth factor receptor 2 binding; protein heterodimerization activity; fibronectin binding; receptor binding; chemoattractant activity
Biological Process: heart morphogenesis; positive regulation of positive chemotaxis; positive regulation of cell adhesion; macrophage differentiation; multicellular organismal development; positive regulation of receptor internalization; cell maturation; basophil chemotaxis; regulation of cell shape; positive regulation of MAP kinase activity; positive chemotaxis; 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; monocyte differentiation; positive regulation of signal transduction; 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; regulation of transcription from RNA polymerase II promoter; patterning of blood vessels; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of angiogenesis; eye photoreceptor cell development; camera-type eye morphogenesis; cell migration during sprouting angiogenesis; branching morphogenesis of a tube; cardiac muscle fiber development; positive regulation of cell division; activation of protein kinase activity; positive regulation of axon extension involved in axon guidance; blood vessel morphogenesis; neuron development; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; surfactant homeostasis; alveolus development; 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; positive regulation of vascular endothelial growth factor receptor signaling pathway; induction of positive chemotaxis; vasculature development; positive regulation of focal adhesion formation; ovarian follicle development; epithelial cell differentiation; positive regulation of cell proliferation; negative regulation of programmed cell death; angiogenesis; cell differentiation; negative regulation of bone resorption; blood vessel development; cell migration; in utero embryonic development; lumen formation; positive regulation of cell motility; positive regulation of peptidyl-serine phosphorylation; cell proliferation; positive regulation of protein kinase B signaling cascade; positive regulation of protein complex assembly; response to hypoxia; artery morphogenesis; blood vessel remodeling; positive regulation of protein amino acid phosphorylation; vascular endothelial growth factor receptor signaling pathway; growth; positive regulation of cell migration; lung development
Reference #:  NP_001020421 (RefSeq)
Alt. Names/Synonyms: OTTMUSP00000017463; OTTMUSP00000017464; OTTMUSP00000022243; Vascular endothelial growth factor A; Vascular permeability factor; Vegf; VEGF-A; Vegf120; Vegf164; Vegf188; Vegfa; VPF
Gene Symbols: Vegfa
Molecular weight: 43,131 Da
Basal Isoelectric point: 9.27  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis
Select Structure to View Below


Protein Structure Not Found.

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


0 253 K324-a EKKSVRGkGkGQkRK
0 254 K326-a KSVRGkGkGQkRKRK
0 254 K329-a RGkGkGQkRKRKKSR

► Hide Isoforms
  VEGF iso4  
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  VEGF iso6  
  VEGF iso10  
- gap
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  VEGF iso14  

► Hide Isoforms
  VEGF iso2  
- gap
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