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VEGFB (human)

Overview VEGFB Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis. Homodimer; disulfide-linked. Can also form heterodimer with VEGF. Expressed in all tissues except liver. Highest levels found in heart, skeletal muscle and pancreas. Belongs to the PDGF/VEGF growth factor family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: Motility/polarity/chemotaxis; Cell cycle regulation; Secreted, signal peptide; Secreted; Cytokine Cellular Component: extracellular space; membrane; extracellular region Molecular Function: heparin binding; protein binding; protein homodimerization activity; growth factor activity; protein heterodimerization activity; vascular endothelial growth factor receptor 1 binding; chemoattractant activity Biological Process: protein amino acid O-linked glycosylation; platelet activation; positive regulation of vascular permeability; positive regulation of vascular endothelial growth factor receptor signaling pathway; induction of positive chemotaxis; positive regulation of protein kinase B signaling cascade; positive regulation of peptidyl-tyrosine phosphorylation; platelet degranulation; positive chemotaxis; positive regulation of cell division; positive regulation of endothelial cell proliferation; negative regulation of neuron apoptosis; vascular endothelial growth factor receptor signaling pathway; blood coagulation; cardiac muscle contraction; negative regulation of apoptosis Reference #:  P49765 (UniProtKB) Alt. Names/Synonyms: Vascular endothelial growth factor B; VEGF-B; VEGF-related factor; VEGFB; VEGFL; VRF Gene Symbols: VEGFB Molecular weight: 21,602 Da Basal Isoelectric point: 8.46  Predict pI for various phosphorylation states CST Pathways:  Angiogenesis Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below VEGFB 2C7W - A/B=31-129 (human) 2VWE - A/B=22-188 (human) 2XAC - A/B=31-129 (human)

STRING  |  Scansite  |  Phospho.ELM  |  Pfam  |  RCSB PDB 2C7W 2VWE 2XAC  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein

	Modification Sites and Domains

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