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Protein Page:
VEGF (rat)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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: Motility/polarity/chemotaxis; Cytokine; Secreted, signal peptide; Secreted
Cellular Component: basement membrane; cell surface; cytoplasm; extracellular region; extracellular space; nucleus; secretory granule
Molecular Function: chemoattractant activity; cytokine activity; extracellular matrix binding; fibronectin binding; growth factor activity; growth factor binding; heparin binding; identical protein binding; platelet-derived growth factor receptor binding; protein heterodimerization activity; protein homodimerization activity; receptor agonist activity; receptor binding; vascular endothelial growth factor receptor 1 binding; vascular endothelial growth factor receptor 2 binding; vascular endothelial growth factor receptor binding
Biological Process: activation of CREB transcription factor; activation of protein kinase activity; aging; alveolus development; angiogenesis; artery morphogenesis; basophil chemotaxis; blood vessel development; blood vessel endothelial cell proliferation during sprouting angiogenesis; blood vessel morphogenesis; blood vessel remodeling; branching morphogenesis of a tube; camera-type eye morphogenesis; cardiac muscle fiber development; cell maturation; cell migration; cell migration during sprouting angiogenesis; cell proliferation; endothelial cell migration; epithelial cell differentiation; eye photoreceptor cell development; female pregnancy; growth; heart morphogenesis; homeostasis of number of cells within a tissue; hyaluronan metabolic process; in utero embryonic development; induction of positive chemotaxis; kidney development; lactation; lumen formation; lung development; lymphangiogenesis; macrophage differentiation; mesoderm development; monocyte differentiation; mRNA stabilization; negative regulation of apoptosis; negative regulation of bone resorption; negative regulation of caspase activity; negative regulation of cell-cell adhesion; negative regulation of fat cell differentiation; negative regulation of programmed cell death; negative regulation of transcription from RNA polymerase II promoter; nervous system development; ovarian follicle development; patterning of blood vessels; positive chemotaxis; positive regulation of angiogenesis; positive regulation of axon extension involved in axon guidance; positive regulation of blood vessel endothelial cell migration; positive regulation of cell adhesion; positive regulation of cell migration; positive regulation of cell motility; positive regulation of cell proliferation; positive regulation of endothelial cell proliferation; positive regulation of epithelial cell proliferation; positive regulation of focal adhesion formation; positive regulation of MAP kinase activity; positive regulation of mesenchymal cell proliferation; positive regulation of neuroblast proliferation; positive regulation of osteoblast differentiation; positive regulation of peptidyl-serine phosphorylation; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of positive chemotaxis; positive regulation of protein amino acid autophosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of protein complex assembly; positive regulation of receptor internalization; positive regulation of signal transduction; positive regulation of smooth muscle cell proliferation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of tyrosine phosphorylation of Stat3 protein; positive regulation of vascular endothelial growth factor receptor signaling pathway; positive regulation of vascular permeability; post-embryonic camera-type eye development; regulation of cell shape; regulation of cGMP metabolic process; regulation of endothelial cell differentiation; regulation of transcription from RNA polymerase II promoter; response to cold; response to estradiol stimulus; response to folic acid; response to hypoxia; response to progesterone stimulus; response to vitamin A; surfactant homeostasis; T-helper 1 type immune response; vascular endothelial growth factor receptor signaling pathway; vasculature development; wound healing
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.
Download PyMol Script
Download ChimeraX Script


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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



 LTP 

LTP: 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.


 HTP 

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


       rat

► Hide Isoforms
 
0 1 I77 CAAGGKPIGAGRSAS
0 1 S82 KPIGAGRSASSGLEK
0 1 S84 IGAGRSASSGLEKPG
0 1 S85 GAGRSASSGLEKPGP
0 2 S161 QESGLPRSPSRRGSA
0 17 K320 DRTKPEKKSVRGkGk
0 253 K325‑ac EKKSVRGkGkGQkRK
0 255 K327‑ac KSVRGkGkGQkRKRK
0 255 K330‑ac RGkGkGQkRKRKKSR
0 1 H344 RFKSWSVHCEPCSER
  VEGF iso2  
I77 CAAGGKPIGAGRSAS
S82 KPIGAGRSASSGLEK
S84 IGAGRSASSGLEKPG
S85 GAGRSASSGLEKPGP
S161 QESGLPRSPSRRGSA
- gap
- gap
- gap
- gap
H320 DRTKPENHCEPCSER
  human

► Hide Isoforms
 
- gap
- gap
- gap
- gap
- gap
K142 DRARQEKKSVRGKGK
K147 EKKSVRGKGKGQKRK
K149 KSVRGKGKGQKRKRK
K152 RGKGKGQKRKRKKSR
Y166 RYKSWSVYVGARCCL
  VEGF iso4  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  VEGF iso6  
- gap
- gap
- gap
- gap
- gap
K142 DRARQEKKSVRGKGK
K147 EKKSVRGKGKGQKRK
K149 KSVRGKGKGQKRKRK
K152 RGKGKGQKRKRKKSR
- gap
  VEGF iso10  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  VEGF iso14  
S77‑p RAGEAEPsGAARsAs
S82‑p EPsGAARsAssGREE
S84‑p sGAARsAssGREEPQ
S85‑p GAARsAssGREEPQP
S162 EESGPPHSPSRRGSA
K322‑ac DRARQEKkSVRGkGk
K327‑ac EKkSVRGkGkGQkRK
K329‑ac kSVRGkGkGQkRKRK
K332‑ac RGkGkGQkRKRKKSR
Y346‑p RYKSWSVyVGARCCL
  mouse

 
I76 CAAGDKPIGAGRSAS
S81 KPIGAGRSASSGLEK
S83 IGAGRSASSGLEKPG
S84 GAGRSASSGLEKPGP
S160‑p QESGLPRsPSRRGSA
K319 DRTKPEKKSVRGkGk
K324‑ac EKKSVRGkGkGQkRK
K326‑ac KSVRGkGkGQkRKRK
K329‑ac RGkGkGQkRKRKKSR
H343 RFKSWSVHCEPCSER
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