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Protein Page:
VEGF (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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; Motility/polarity/chemotaxis; Cytokine; Secreted, signal peptide
Cellular Component: proteinaceous extracellular matrix; extracellular space; cell surface; membrane; cytoplasm; extracellular region; secretory granule
Molecular Function: heparin binding; identical protein binding; protein homodimerization activity; growth factor activity; extracellular matrix binding; cytokine activity; platelet-derived growth factor receptor binding; 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; chemoattractant activity
Biological Process: heart morphogenesis; positive regulation of positive chemotaxis; positive regulation of cell adhesion; macrophage differentiation; positive regulation of leukocyte migration; cell maturation; positive regulation of receptor internalization; basophil chemotaxis; regulation of cell shape; positive regulation of MAP kinase activity; positive chemotaxis; positive regulation of mesenchymal cell proliferation; mesoderm development; kidney development; platelet activation; nervous system development; positive regulation of neuroblast proliferation; monocyte differentiation; 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; eye photoreceptor cell development; positive regulation of angiogenesis; 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; positive regulation of transcription from RNA polymerase II promoter; positive regulation of endothelial cell proliferation; surfactant homeostasis; positive regulation of epithelial cell proliferation; negative regulation of apoptosis; lactation; post-embryonic camera-type eye development; negative regulation of caspase activity; negative regulation of transcription from RNA polymerase II promoter; positive regulation of vascular endothelial growth factor receptor signaling pathway; induction of positive chemotaxis; platelet degranulation; positive regulation of focal adhesion formation; ovarian follicle development; epithelial cell differentiation; positive regulation of cell proliferation; angiogenesis; vasculogenesis; in utero embryonic development; lumen formation; positive regulation of cell motility; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein complex assembly; response to hypoxia; artery morphogenesis; positive regulation of protein amino acid phosphorylation; vascular endothelial growth factor receptor signaling pathway; blood coagulation; positive regulation of cell migration; lung development; growth
Reference #:  P15692 (UniProtKB)
Alt. Names/Synonyms: Vascular endothelial growth factor A; Vascular permeability factor; VEGF-A; VEGFA
Gene Symbols: VEGFA
Molecular weight: 27,042 Da
Basal Isoelectric point: 9.21  Predict pI for various phosphorylation states
CST Pathways:  Angiogenesis
Select Structure to View Below

VEGF

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 

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.


       human

► Hide Isoforms
 
0 1 - gap
0 1 - gap
0 1 - gap
0 1 - gap
0 17 K142 DRARQEKKSVRGKGK
0 253 K147 EKKSVRGKGKGQKRK
0 254 K149 KSVRGKGKGQKRKRK
0 254 K152 RGKGKGQKRKRKKSR
0 1 Y166 RYKSWSVYVGARCCL
  VEGF iso4  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  VEGF iso6  
- gap
- gap
- gap
- gap
K142 DRARQEKKSVRGKGK
K147 EKKSVRGKGKGQKRK
K149 KSVRGKGKGQKRKRK
K152 RGKGKGQKRKRKKSR
- gap
  VEGF iso10  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  VEGF iso14  
S77-p RAGEAEPsGAARsAs
S82-p EPsGAARsAssGREE
S84-p sGAARsAssGREEPQ
S85-p GAARsAssGREEPQP
K322-ac DRARQEKkSVRGkGk
K327-ac EKkSVRGkGkGQkRK
K329-ac kSVRGkGkGQkRKRK
K332-ac RGkGkGQkRKRKKSR
Y346-p RYKSWSVyVGARCCL
  mouse

 
I76 CAAGDKPIGAGRSAS
S81 KPIGAGRSASSGLEK
S83 IGAGRSASSGLEKPG
S84 GAGRSASSGLEKPGP
K319 DRTKPEKKSVRGkGk
K324-ac EKKSVRGkGkGQkRK
K326-ac KSVRGkGkGQkRKRK
K329-ac RGkGkGQkRKRKKSR
H343 RFKSWSVHCEPCSER
  rat

► Hide Isoforms
 
I77 CAAGGKPIGAGRSAS
S82 KPIGAGRSASSGLEK
S84 IGAGRSASSGLEKPG
S85 GAGRSASSGLEKPGP
K320 DRTKPEKKSVRGkGk
K325-ac EKKSVRGkGkGQkRK
K327-ac KSVRGkGkGQkRKRK
K330-ac RGkGkGQkRKRKKSR
H344 RFKSWSVHCEPCSER
  VEGF iso2  
I77 CAAGGKPIGAGRSAS
S82 KPIGAGRSASSGLEK
S84 IGAGRSASSGLEKPG
S85 GAGRSASSGLEKPGP
- gap
- gap
- gap
- gap
H320 DRTKPENHCEPCSER
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