Vascular endothelial growth factor B
Details
- Name
- Vascular endothelial growth factor B
- Kind
- protein
- Synonyms
- VEGF-B
- VEGF-related factor
- VRF
- Gene Name
- VEGFB
- UniProtKB Entry
- P49765Swiss-Prot
- Organism
- Humans
- NCBI Taxonomy ID
- 9606
- Amino acid sequence
>lcl|BSEQ0008587|Vascular endothelial growth factor B MSPLLRRLLLAALLQLAPAQAPVSQPDAPGHQRKVVSWIDVYTRATCQPREVVVPLTVEL MGTVAKQLVPSCVTVQRCGGCCPDDGLECVPTGQHQVRMQILMIRYPSSQLGEMSLEEHS QCECRPKKKDSAVKPDRAATPHHRPQPRSVPGWDSAPGAPSPADITHPTPAPGPSAHAAP STTSALTPGPAAAAADAAASSVAKGGA
- Number of residues
- 207
- Molecular Weight
- 21601.56
- Theoretical pI
- Not Available
- GO Classification
- Functionschemoattractant activity / heparin binding / vascular endothelial growth factor receptor 1 bindingProcessescardiac muscle contraction / coronary vasculature development / induction of positive chemotaxis / negative regulation of apoptotic process / negative regulation of gene expression / negative regulation of neuron apoptotic process / positive regulation of cell division / positive regulation of endothelial cell proliferation / positive regulation of ERK1 and ERK2 cascade / positive regulation of mast cell chemotaxis / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of vascular endothelial growth factor receptor signaling pathway / positive regulation of vascular wound healing / protein O-linked glycosylation / vascular endothelial growth factor receptor signaling pathwayComponentsextracellular region / extracellular space / membrane / platelet alpha granule lumen
- General Function
- 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
- Specific Function
- chemoattractant activity
- Pfam Domain Function
- PDGF (PF00341)
- Signal Regions
- 1-21
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0017521|Vascular endothelial growth factor B (VEGFB) ATGAGCCCTCTGCTCCGCCGCCTGCTGCTCGCCGCACTCCTGCAGCTGGCCCCCGCCCAG GCCCCTGTCTCCCAGCCTGATGCCCCTGGCCACCAGAGGAAAGTGGTGTCATGGATAGAT GTGTATACTCGCGCTACCTGCCAGCCCCGGGAGGTGGTGGTGCCCTTGACTGTGGAGCTC ATGGGCACCGTGGCCAAACAGCTGGTGCCCAGCTGCGTGACTGTGCAGCGCTGTGGTGGC TGCTGCCCTGACGATGGCCTGGAGTGTGTGCCCACTGGGCAGCACCAAGTCCGGATGCAG ATCCTCATGATCCGGTACCCGAGCAGTCAGCTGGGGGAGATGTCCCTGGAAGAACACAGC CAGTGTGAATGCAGACCTAAAAAAAAGGACAGTGCTGTGAAGCCAGACAGCCCCAGGCCC CTCTGCCCACGCTGCACCCAGCACCACCAGCGCCCTGACCCCCGGACCTGCCGCTGCCGC TGCCGACGCCGCAGCTTCCTCCGTTGCCAAGGGCGGGGCTTAGAGCTCAACCCAGACACC TGCAGGTGCCGGAAGCTGCGAAGGTGA
- Chromosome Location
- 11
- Locus
- 11q13.1
- External Identifiers
Resource Link UniProtKB ID P49765 UniProtKB Entry Name VEGFB_HUMAN GeneCard ID VEGFB HGNC ID HGNC:12681 PDB ID(s) 2C7W, 2VWE, 2XAC, 6TKK KEGG ID hsa:7423 NCBI Gene ID 7423 - General References
- Grimmond S, Lagercrantz J, Drinkwater C, Silins G, Townson S, Pollock P, Gotley D, Carson E, Rakar S, Nordenskjold M, Ward L, Hayward N, Weber G: Cloning and characterization of a novel human gene related to vascular endothelial growth factor. Genome Res. 1996 Feb;6(2):124-31. [Article]
- Olofsson B, Pajusola K, von Euler G, Chilov D, Alitalo K, Eriksson U: Genomic organization of the mouse and human genes for vascular endothelial growth factor B (VEGF-B) and characterization of a second splice isoform. J Biol Chem. 1996 Aug 9;271(32):19310-7. [Article]
- Olofsson B, Pajusola K, Kaipainen A, von Euler G, Joukov V, Saksela O, Orpana A, Pettersson RF, Alitalo K, Eriksson U: Vascular endothelial growth factor B, a novel growth factor for endothelial cells. Proc Natl Acad Sci U S A. 1996 Mar 19;93(6):2576-81. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Iyer S, Scotney PD, Nash AD, Ravi Acharya K: Crystal structure of human vascular endothelial growth factor-B: identification of amino acids important for receptor binding. J Mol Biol. 2006 May 26;359(1):76-85. Epub 2006 Apr 17. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Aflibercept approved yes target inhibitorbinder Details NM-3 investigational yes target inhibitor Details TG-100801 investigational yes target inhibitor Details Risuteganib investigational yes target modulator Details Squalamine investigational yes target modulator Details