Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Vascular endothelial growth factor A (VEGF-A) (Vascular permeability factor) (VPF)

 VEGFA_HUMAN             Reviewed;         232 AA.
P15692; B5BU86; H0Y2S8; H0Y407; H0Y414; H0Y462; H0Y8N2; H3BLW7;
O60720; O75875; Q074Z4; Q16889; Q5UB46; Q6P0P5; Q96KJ0; Q96L82;
Q96NW5; Q9H1W8; Q9H1W9; Q9UH58; Q9UL23;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
16-NOV-2001, sequence version 2.
30-AUG-2017, entry version 223.
RecName: Full=Vascular endothelial growth factor A;
Short=VEGF-A;
AltName: Full=Vascular permeability factor;
Short=VPF;
Flags: Precursor;
Name=VEGFA; Synonyms=VEGF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF189 AND VEGF165).
PubMed=2479986; DOI=10.1126/science.2479986;
Leung D.W., Cachianes G., Kuang W.-J., Goeddel D.V., Ferrara N.;
"Vascular endothelial growth factor is a secreted angiogenic
mitogen.";
Science 246:1306-1309(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF189), AND PARTIAL PROTEIN
SEQUENCE.
PubMed=2479987; DOI=10.1126/science.2479987;
Keck P.J., Hauser S.D., Krivi G., Sanzo K., Warren T., Feder J.,
Connolly D.T.;
"Vascular permeability factor, an endothelial cell mitogen related to
PDGF.";
Science 246:1309-1312(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM VEGF189).
PubMed=1711045;
Tischer E., Mitchell R., Hartman T., Silva M., Gospodarowicz D.,
Fiddes J.C., Abraham J.A.;
"The human gene for vascular endothelial growth factor. Multiple
protein forms are encoded through alternative exon splicing.";
J. Biol. Chem. 266:11947-11954(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM VEGF206).
PubMed=1791831; DOI=10.1210/mend-5-12-1806;
Houck K.A., Ferrara N., Winer J., Cachianes G., Li B., Leung D.W.;
"The vascular endothelial growth factor family: identification of a
fourth molecular species and characterization of alternative splicing
of RNA.";
Mol. Endocrinol. 5:1806-1814(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
PubMed=1567395; DOI=10.1016/S0006-291X(05)80313-4;
Weindel K., Marme D., Weich H.A.;
"AIDS-associated Kaposi's sarcoma cells in culture express vascular
endothelial growth factor.";
Biochem. Biophys. Res. Commun. 183:1167-1174(1992).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF145).
PubMed=9054410; DOI=10.1074/jbc.272.11.7151;
Poltorak Z., Cohen T., Sivan R., Kandelis Y., Spira G., Vlodavsky I.,
Keshet E., Neufeld G.;
"VEGF145, a secreted vascular endothelial growth factor isoform that
binds to extracellular matrix.";
J. Biol. Chem. 272:7151-7158(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF183).
TISSUE=Kidney;
PubMed=9878851; DOI=10.1016/S0167-4781(98)00240-1;
Lei J., Jiang A., Pei D.;
"Identification and characterization of a new splicing variant of
vascular endothelial growth factor: VEGF183.";
Biochim. Biophys. Acta 1443:400-406(1998).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-VEGF165).
TISSUE=Mammary gland;
PubMed=9450968; DOI=10.1091/mbc.9.2.469;
Claffey K.P., Shih S.-C., Mullen A., Dziennis S., Cusick J.L.,
Abrams K.R., Lee S.W., Detmar M.;
"Identification of a human VPF/VEGF 3' untranslated region mediating
hypoxia-induced mRNA stability.";
Mol. Biol. Cell 9:469-481(1998).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF148).
TISSUE=Renal glomerulus;
PubMed=10464055; DOI=10.1042/cs0970303;
Whittle C.J., Gillespie K.M., Harrison R., Mathieson P.W.,
Harper S.J.;
"Heterogeneous vascular endothelial growth factor (VEGF) isoform mRNA
and receptor mRNA expression in human glomeruli, and the
identification of VEGF148 mRNA, a novel truncated splice variant.";
Clin. Sci. 97:303-312(1999).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165B).
TISSUE=Kidney;
PubMed=12124351;
Bates D.O., Cui T.-G., Doughty J.M., Winkler M., Sugiono M.,
Shields J.D., Peat D., Gillatt D., Harper S.J.;
"VEGF165b, an inhibitory splice variant of vascular endothelial growth
factor, is down-regulated in renal cell carcinoma.";
Cancer Res. 62:4123-4131(2002).
[11]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
TISSUE=Hemangioendothelioma;
Murata H., Fukushima J., Hattori S., Okuda K., Yanagi H.;
"Human cDNA for the vascular endothelial growth factor isoform
VEGF165.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF121).
Sato J.D., Whitney R.G.;
"Human cDNA for vascular endothelial growth factor isoform VEGF121.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
Liu J., Peng X., Yuan J., Qiang B.;
"Cloning of vascular endothelial growth factor (VEGF) cDNA.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
TISSUE=Heart;
Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Zheng M., Tan H.H., Lin S.G.;
"Cloning and identification of vascular endothelial growth factor
isoform VEGF165.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
Koul S., Johnson T., Meacham R.B., Koul H.K.;
"Cloning and characterization of VEGF from LNCaP cells, a line of
prostate cancer cells.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF111).
Mineur P.J., Colige A.C., Lambert C.A.;
"VEGF111, a new VEGF-A variant lacking exons 5, 6 and 7.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[17]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF165).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[18]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[19]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[20]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L-VEGF121).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[21]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-232.
SeattleSNPs variation discovery resource;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[22]
PROTEIN SEQUENCE OF 27-41.
PubMed=7678805; DOI=10.1111/j.1432-1033.1993.tb19865.x;
Fiebich B.L., Jaeger B., Schoellmann C., Weindel K., Wilting J.,
Kochs G., Marme D., Hug H., Weich H.A.;
"Synthesis and assembly of functionally active human vascular
endothelial growth factor homodimers in insect cells.";
Eur. J. Biochem. 211:19-26(1993).
[23]
PROTEIN SEQUENCE OF 27-41.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[24]
PRELIMINARY PROTEIN SEQUENCE OF 27-36; 43-50 AND 59-81.
PubMed=2584205;
Connolly D.T., Olander J.V., Heuvelman D., Nelson R., Monsell R.,
Siegel N., Haymore B.L., Leimgruber R., Feder J.;
"Human vascular permeability factor. Isolation from U937 cells.";
J. Biol. Chem. 264:20017-20024(1989).
[25]
NUCLEOTIDE SEQUENCE [MRNA] OF 114-209 (ISOFORM VEGF183).
TISSUE=Retina;
PubMed=10067980;
Jingjing L., Xue Y., Agarwal N., Roque R.S.;
"Human Muller cells express VEGF183, a novel spliced variant of
vascular endothelial growth factor.";
Invest. Ophthalmol. Vis. Sci. 40:752-759(1999).
[26]
ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING,
AND SUBCELLULAR LOCATION.
PubMed=11563986; DOI=10.1042/0264-6021:3590219;
Tee M.K., Jaffe R.B.;
"A precursor form of vascular endothelial growth factor arises by
initiation from an upstream in-frame CUG codon.";
Biochem. J. 359:219-226(2001).
[27]
FUNCTION.
PubMed=11427521;
Murphy J.F., Fitzgerald D.J.;
"Vascular endothelial growth factor induces cyclooxygenase-dependent
proliferation of endothelial cells via the VEGF-2 receptor.";
FASEB J. 15:1667-1669(2001).
[28]
ALTERNATIVE SPLICING (ISOFORM L-VEGF189), PROCESSING, AND SUBCELLULAR
LOCATION.
PubMed=11731620; DOI=10.1210/mend.15.12.0738;
Huez I., Bornes S., Bresson D., Creancier L., Prats H.;
"New vascular endothelial growth factor isoform generated by internal
ribosome entry site-driven CUG translation initiation.";
Mol. Endocrinol. 15:2197-2210(2001).
[29]
INVOLVEMENT IN MVCD1.
PubMed=11978667; DOI=10.2337/diabetes.51.5.1635;
Awata T., Inoue K., Kurihara S., Ohkubo T., Watanabe M., Inukai K.,
Inoue I., Katayama S.;
"A common polymorphism in the 5'-untranslated region of the VEGF gene
is associated with diabetic retinopathy in type 2 diabetes.";
Diabetes 51:1635-1639(2002).
[30]
FUNCTION (ISOFORM VEGF165B).
PubMed=15520188; DOI=10.1158/0008-5472.CAN-04-0934;
Woolard J., Wang W.-Y., Bevan H.S., Qiu Y., Morbidelli L.,
Pritchard-Jones R.O., Cui T.-G., Sugiono M., Waine E., Perrin R.,
Foster R., Digby-Bell J., Shields J.D., Whittles C.E., Mushens R.E.,
Gillatt D.A., Ziche M., Harper S.J., Bates D.O.;
"VEGF165b, an inhibitory vascular endothelial growth factor splice
variant: mechanism of action, in vivo effect on angiogenesis and
endogenous protein expression.";
Cancer Res. 64:7822-7835(2004).
[31]
ALTERNATIVE SPLICING (ISOFORMS L-VEGF121; L-VEGF165 AND L-VEGF189).
PubMed=14764596; DOI=10.1074/jbc.M308410200;
Bornes S., Boulard M., Hieblot C., Zanibellato C., Iacovoni J.S.,
Prats H., Touriol C.;
"Control of the vascular endothelial growth factor internal ribosome
entry site (IRES) activity and translation initiation by alternatively
spliced coding sequences.";
J. Biol. Chem. 279:18717-18726(2004).
[32]
ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING,
AND SUBCELLULAR LOCATION.
PubMed=15896327; DOI=10.1016/j.bbrc.2005.04.123;
Rosenbaum-Dekel Y., Fuchs A., Yakirevich E., Azriel A., Mazareb S.,
Resnick M.B., Levi B.Z.;
"Nuclear localization of long-VEGF is associated with hypoxia and
tumor angiogenesis.";
Biochem. Biophys. Res. Commun. 332:271-278(2005).
[33]
FUNCTION IN CELL MIGRATION.
PubMed=16489009; DOI=10.1158/0008-5472.CAN-05-2217;
Dixelius J., Olsson A.K., Thulin A., Lee C., Johansson I.,
Claesson-Welsh L.;
"Minimal active domain and mechanism of action of the angiogenesis
inhibitor histidine-rich glycoprotein.";
Cancer Res. 66:2089-2097(2006).
[34]
INTERACTION WITH NRP1.
PubMed=26503042; DOI=10.1038/nature15510;
He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
Dumitru C.D., Lettieri K., Shubayev V., Jordanova A.,
Guergueltcheva V., Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
"CMT2D neuropathy is linked to the neomorphic binding activity of
glycyl-tRNA synthetase.";
Nature 526:710-714(2015).
[35]
ERRATUM.
PubMed=26789244; DOI=10.1038/nature16499;
He W., Bai G., Zhou H., Wei N., White N.M., Lauer J., Liu H., Shi Y.,
Dan Dumitru C., Lettieri K., Shubayev V., Jordanova A.,
Guergueltcheva V., Griffin P.R., Burgess R.W., Pfaff S.L., Yang X.L.;
"Corrigendum: CMT2D neuropathy is linked to the neomorphic binding
activity of glycyl-tRNA synthetase.";
Nature 532:402-402(2016).
[36]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=22009797; DOI=10.1530/ERC-11-0211;
Shan B., Gerez J., Haedo M., Fuertes M., Theodoropoulou M.,
Buchfelder M., Losa M., Stalla G.K., Arzt E., Renner U.;
"RSUME is implicated in HIF-1-induced VEGF-A production in pituitary
tumour cells.";
Endocr. Relat. Cancer 19:13-27(2012).
[37]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-135.
PubMed=9207067; DOI=10.1073/pnas.94.14.7192;
Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C.,
de Vos A.M.;
"Vascular endothelial growth factor: crystal structure and functional
mapping of the kinase domain receptor binding site.";
Proc. Natl. Acad. Sci. U.S.A. 94:7192-7197(1997).
[38]
STRUCTURE BY NMR OF 34-135.
PubMed=9336848; DOI=10.1002/pro.5560061020;
Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A.,
Starovasnik M.A.;
"1H, 13C, and 15N backbone assignment and secondary structure of the
receptor-binding domain of vascular endothelial growth factor.";
Protein Sci. 6:2250-2260(1997).
[39]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 34-135.
PubMed=9351807; DOI=10.1016/S0969-2126(97)00284-0;
Muller Y.A., Christinger H.W., Keyt B.A., de Vos A.M.;
"The crystal structure of vascular endothelial growth factor (VEGF)
refined to 1.93-A resolution: multiple copy flexibility and receptor
binding.";
Structure 5:1325-1338(1997).
[40]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-134.
PubMed=9922142; DOI=10.1021/bi9819327;
Wiesmann C., Christinger H.W., Cochran A.G., Cunningham B.C.,
Fairbrother W.J., Keenan C.J., Meng G., de Vos A.M.;
"Crystal structure of the complex between VEGF and a receptor-blocking
peptide.";
Biochemistry 37:17765-17772(1998).
[41]
STRUCTURE BY NMR OF 137-215.
PubMed=9634701; DOI=10.1016/S0969-2126(98)00065-3;
Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A.,
Starovasnik M.A.;
"Solution structure of the heparin-binding domain of vascular
endothelial growth factor.";
Structure 6:637-648(1998).
-!- FUNCTION: 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. Binding to NRP1 receptor initiates a signaling pathway
needed for motor neuron axon guidance and cell body migration,
including for the caudal migration of facial motor neurons from
rhombomere 4 to rhombomere 6 during embryonic development (By
similarity). {ECO:0000250|UniProtKB:Q00731,
ECO:0000269|PubMed:11427521, ECO:0000269|PubMed:16489009}.
-!- SUBUNIT: Homodimer; disulfide-linked. Also found as heterodimer
with PGF (By similarity). Interacts with NRP1 (PubMed:26503042).
{ECO:0000250, ECO:0000269|PubMed:26503042}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-1026643, EBI-1026643;
P17948:FLT1; NbExp=4; IntAct=EBI-1026643, EBI-1026718;
P35968:KDR; NbExp=6; IntAct=EBI-1026691, EBI-1005487;
O14786:NRP1; NbExp=4; IntAct=EBI-1026643, EBI-1187100;
O14786-2:NRP1; NbExp=4; IntAct=EBI-1026691, EBI-6285281;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11563986,
ECO:0000269|PubMed:11731620, ECO:0000269|PubMed:15896327}.
Note=VEGF121 is acidic and freely secreted. VEGF165 is more basic,
has heparin-binding properties and, although a signicant
proportion remains cell-associated, most is freely secreted.
VEGF189 is very basic, it is cell-associated after secretion and
is bound avidly by heparin and the extracellular matrix, although
it may be released as a soluble form by heparin, heparinase or
plasmin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing, Alternative initiation; Named isoforms=17;
Comment=Additional isoforms seem to exist.;
Name=VEGF206;
IsoId=P15692-1; Sequence=Displayed;
Name=VEGF189;
IsoId=P15692-2; Sequence=VSP_004622;
Name=VEGF183;
IsoId=P15692-3; Sequence=VSP_004621;
Name=VEGF165; Synonyms=VEGF;
IsoId=P15692-4; Sequence=VSP_004618, VSP_004619;
Name=VEGF148;
IsoId=P15692-5; Sequence=VSP_004618, VSP_004619, VSP_004624,
VSP_004625;
Name=VEGF145;
IsoId=P15692-6; Sequence=VSP_004623;
Name=VEGF165B;
IsoId=P15692-8; Sequence=VSP_004618, VSP_004619, VSP_014783;
Name=VEGF121;
IsoId=P15692-9; Sequence=VSP_004620;
Note=No experimental confirmation available.;
Name=VEGF111;
IsoId=P15692-10; Sequence=VSP_026781;
Note=No experimental confirmation available.;
Name=L-VEGF165;
IsoId=P15692-11; Sequence=VSP_038745, VSP_004618, VSP_004619;
Note=Produced by alternative promoter usage and alternative
initiation. Starts at an alternative upstream CUG codon.
Post-translationally processed to produce the secreted VEGF
peptide and a N-terminal peptide N-VEGF. The unprocessed protein
and the N-VEGF peptide may localize to the nucleus (Ref.32), the
endoplasmic reticulum and the Golgi (Ref.28) or the
extracellular matrix (Ref.26). {ECO:0000305|PubMed:11563986,
ECO:0000305|PubMed:11731620, ECO:0000305|PubMed:15896327};
Name=L-VEGF121;
IsoId=P15692-12; Sequence=VSP_038745, VSP_004620;
Note=Produced by alternative promoter usage and alternative
initiation. Starts at an alternative upstream CUG codon.
Post-translationally processed to produce the secreted VEGF
peptide and a N-terminal peptide N-VEGF. The unprocessed protein
and the N-VEGF peptide may localize to the nucleus (Ref.32), the
endoplasmic reticulum and the Golgi (Ref.28) or the
extracellular matrix (Ref.26). {ECO:0000305|PubMed:11563986,
ECO:0000305|PubMed:11731620, ECO:0000305|PubMed:15896327};
Name=L-VEGF189;
IsoId=P15692-13; Sequence=VSP_038745, VSP_004622;
Note=Produced by alternative promoter usage and alternative
initiation. Starts at an alternative upstream CUG codon.
Post-translationally processed to produce the secreted VEGF
peptide and a N-terminal peptide N-VEGF. The unprocessed protein
and the N-VEGF peptide may localize to the nucleus (Ref.32), the
endoplasmic reticulum and the Golgi (Ref.28) or the
extracellular matrix (Ref.26). {ECO:0000305|PubMed:11563986,
ECO:0000305|PubMed:11731620, ECO:0000305|PubMed:15896327};
Name=L-VEGF206;
IsoId=P15692-14; Sequence=VSP_038745;
Note=Gene prediction based on EST data. Produced by alternative
promoter usage and alternative initiation. Starts at an
alternative upstream CUG codon.;
Name=15;
IsoId=P15692-15; Sequence=VSP_038745, VSP_054111, VSP_014783;
Note=Starts at an alternative upstream CUG codon.;
Name=16;
IsoId=P15692-16; Sequence=VSP_038745, VSP_004621;
Note=Starts at an alternative upstream CUG codon.;
Name=17;
IsoId=P15692-17; Sequence=VSP_038745, VSP_054111, VSP_004624,
VSP_004625;
Note=Starts at an alternative upstream CUG codon.;
Name=18;
IsoId=P15692-18; Sequence=VSP_038745, VSP_026781;
Note=Starts at an alternative upstream CUG codon.;
-!- TISSUE SPECIFICITY: Isoform VEGF189, isoform VEGF165 and isoform
VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145
are not widely expressed. A higher level expression seen in
pituitary tumors as compared to the pituitary gland.
{ECO:0000269|PubMed:22009797}.
-!- INDUCTION: By hypoxia. Regulated by growth factors, cytokines,
gonadotropins, nitric oxide, hypoglycemia and oncogenic mutations.
{ECO:0000269|PubMed:22009797}.
-!- DISEASE: Microvascular complications of diabetes 1 (MVCD1)
[MIM:603933]: 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. {ECO:0000269|PubMed:11978667}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC63102.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAC63143.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=CAC19512.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=CAC19516.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=VEGF entry;
URL="https://en.wikipedia.org/wiki/Vascular_endothelial_growth_factor";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/vegf/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M32977; AAA35789.1; -; mRNA.
EMBL; M27281; AAA36807.1; -; mRNA.
EMBL; M63978; AAA36804.1; -; Genomic_DNA.
EMBL; M63971; AAA36804.1; JOINED; Genomic_DNA.
EMBL; M63972; AAA36804.1; JOINED; Genomic_DNA.
EMBL; M63973; AAA36804.1; JOINED; Genomic_DNA.
EMBL; M63974; AAA36804.1; JOINED; Genomic_DNA.
EMBL; M63975; AAA36804.1; JOINED; Genomic_DNA.
EMBL; M63976; AAA36804.1; JOINED; Genomic_DNA.
EMBL; M63977; AAA36804.1; JOINED; Genomic_DNA.
EMBL; S85192; AAC63102.1; ALT_INIT; mRNA.
EMBL; AH006909; AAC63101.1; -; Genomic_DNA.
EMBL; X62568; CAA44447.1; -; mRNA.
EMBL; AJ010438; CAA09179.1; -; mRNA.
EMBL; AF022375; AAC63143.1; ALT_SEQ; mRNA.
EMBL; AF091352; AAD55345.1; -; mRNA.
EMBL; AF430806; AAL27435.1; -; mRNA.
EMBL; AB021221; BAA78418.1; -; mRNA.
EMBL; AF214570; AAF19659.1; -; mRNA.
EMBL; AY047581; AAK95847.1; -; mRNA.
EMBL; AF486837; AAM03108.1; -; mRNA.
EMBL; AY766116; AAV34601.1; -; mRNA.
EMBL; DQ229900; ABB58912.1; -; mRNA.
EMBL; AB451322; BAG70136.1; -; mRNA.
EMBL; AB451451; BAG70265.1; -; mRNA.
EMBL; AL136131; CAC19512.2; ALT_SEQ; Genomic_DNA.
EMBL; AL136131; CAC19513.2; -; Genomic_DNA.
EMBL; AL136131; CAC19515.2; -; Genomic_DNA.
EMBL; AL136131; CAC19516.2; ALT_SEQ; Genomic_DNA.
EMBL; CH471081; EAX04229.1; -; Genomic_DNA.
EMBL; BC065522; AAH65522.2; -; mRNA.
EMBL; AF437895; AAL27630.1; -; Genomic_DNA.
EMBL; AF062645; AAC16730.1; -; mRNA.
CCDS; CCDS34457.1; -. [P15692-14]
CCDS; CCDS34458.1; -. [P15692-11]
CCDS; CCDS47432.1; -. [P15692-15]
CCDS; CCDS47433.1; -. [P15692-16]
CCDS; CCDS47434.1; -. [P15692-12]
CCDS; CCDS47435.1; -. [P15692-17]
CCDS; CCDS4907.2; -. [P15692-13]
CCDS; CCDS55007.1; -. [P15692-18]
CCDS; CCDS55008.1; -. [P15692-3]
CCDS; CCDS55009.1; -. [P15692-2]
CCDS; CCDS55010.1; -. [P15692-1]
CCDS; CCDS55011.1; -. [P15692-5]
CCDS; CCDS55012.1; -. [P15692-4]
CCDS; CCDS55013.1; -. [P15692-8]
CCDS; CCDS55014.1; -. [P15692-9]
CCDS; CCDS55015.1; -. [P15692-10]
PIR; A41551; A41551.
RefSeq; NP_001020537.2; NM_001025366.2. [P15692-14]
RefSeq; NP_001020538.2; NM_001025367.2. [P15692-16]
RefSeq; NP_001020539.2; NM_001025368.2. [P15692-11]
RefSeq; NP_001020540.2; NM_001025369.2. [P15692-17]
RefSeq; NP_001020541.2; NM_001025370.2. [P15692-12]
RefSeq; NP_001028928.1; NM_001033756.2. [P15692-15]
RefSeq; NP_001165093.1; NM_001171622.1. [P15692-18]
RefSeq; NP_001165094.1; NM_001171623.1. [P15692-1]
RefSeq; NP_001165095.1; NM_001171624.1. [P15692-2]
RefSeq; NP_001165096.1; NM_001171625.1. [P15692-3]
RefSeq; NP_001165097.1; NM_001171626.1. [P15692-4]
RefSeq; NP_001165098.1; NM_001171627.1. [P15692-5]
RefSeq; NP_001165099.1; NM_001171628.1. [P15692-9]
RefSeq; NP_001165100.1; NM_001171629.1. [P15692-8]
RefSeq; NP_001165101.1; NM_001171630.1. [P15692-10]
RefSeq; NP_001191313.1; NM_001204384.1. [P15692-6]
RefSeq; NP_001191314.1; NM_001204385.1.
RefSeq; NP_001273973.1; NM_001287044.1.
RefSeq; NP_001303939.1; NM_001317010.1.
RefSeq; NP_003367.4; NM_003376.5. [P15692-13]
UniGene; Hs.73793; -.
PDB; 1BJ1; X-ray; 2.40 A; V/W=34-135.
PDB; 1CZ8; X-ray; 2.40 A; V/W=40-133.
PDB; 1FLT; X-ray; 1.70 A; V/W=38-135.
PDB; 1KAT; NMR; -; V/W=37-135.
PDB; 1KMX; NMR; -; A=183-232.
PDB; 1MJV; X-ray; 2.10 A; A/B=40-134.
PDB; 1MKG; X-ray; 2.50 A; A/B/C/D=40-134.
PDB; 1MKK; X-ray; 1.32 A; A/B=40-134.
PDB; 1QTY; X-ray; 2.70 A; R/S/V/W=34-135.
PDB; 1TZH; X-ray; 2.60 A; V/W=34-135.
PDB; 1TZI; X-ray; 2.80 A; V=34-135.
PDB; 1VGH; NMR; -; A=180-232.
PDB; 1VPF; X-ray; 2.50 A; A/B/C/D=34-135.
PDB; 1VPP; X-ray; 1.90 A; V/W=34-135.
PDB; 2FJG; X-ray; 2.80 A; V/W=34-135.
PDB; 2FJH; X-ray; 3.10 A; V/W=34-135.
PDB; 2QR0; X-ray; 3.50 A; C/D/I/J/O/P/U/V=39-135.
PDB; 2VGH; NMR; -; A=182-232.
PDB; 2VPF; X-ray; 1.93 A; A/B/C/D/E/F/G/H=34-135.
PDB; 3BDY; X-ray; 2.60 A; V=34-135.
PDB; 3P9W; X-ray; 2.41 A; A/C/E/G=35-138.
PDB; 3QTK; X-ray; 1.85 A; A/B/C/D/E/F=34-135.
PDB; 3S1B; X-ray; 2.90 A; V=38-133.
PDB; 3S1K; X-ray; 2.55 A; V/W=34-135.
PDB; 3V2A; X-ray; 3.20 A; A=27-140.
PDB; 4DEQ; X-ray; 2.65 A; A/B=183-232.
PDB; 4GLN; X-ray; 1.60 A; E/F=34-135.
PDB; 4GLS; X-ray; 1.60 A; E/F=34-135.
PDB; 4KZN; X-ray; 1.71 A; A=39-135.
PDB; 4QAF; X-ray; 1.80 A; C/D=34-135.
PDB; 4WPB; X-ray; 3.11 A; A/B=34-135.
PDB; 4ZFF; X-ray; 2.75 A; C/D=37-135.
PDB; 5DN2; X-ray; 1.95 A; E/F/G=205-232.
PDB; 5FV1; X-ray; 2.70 A; V/W=27-136.
PDB; 5FV2; X-ray; 3.45 A; V/W/X=27-136.
PDB; 5HHC; X-ray; 2.10 A; A/B=34-135.
PDB; 5HHD; X-ray; 2.10 A; A/B=34-135.
PDB; 5T89; X-ray; 4.00 A; V/W=27-155.
PDBsum; 1BJ1; -.
PDBsum; 1CZ8; -.
PDBsum; 1FLT; -.
PDBsum; 1KAT; -.
PDBsum; 1KMX; -.
PDBsum; 1MJV; -.
PDBsum; 1MKG; -.
PDBsum; 1MKK; -.
PDBsum; 1QTY; -.
PDBsum; 1TZH; -.
PDBsum; 1TZI; -.
PDBsum; 1VGH; -.
PDBsum; 1VPF; -.
PDBsum; 1VPP; -.
PDBsum; 2FJG; -.
PDBsum; 2FJH; -.
PDBsum; 2QR0; -.
PDBsum; 2VGH; -.
PDBsum; 2VPF; -.
PDBsum; 3BDY; -.
PDBsum; 3P9W; -.
PDBsum; 3QTK; -.
PDBsum; 3S1B; -.
PDBsum; 3S1K; -.
PDBsum; 3V2A; -.
PDBsum; 4DEQ; -.
PDBsum; 4GLN; -.
PDBsum; 4GLS; -.
PDBsum; 4KZN; -.
PDBsum; 4QAF; -.
PDBsum; 4WPB; -.
PDBsum; 4ZFF; -.
PDBsum; 5DN2; -.
PDBsum; 5FV1; -.
PDBsum; 5FV2; -.
PDBsum; 5HHC; -.
PDBsum; 5HHD; -.
PDBsum; 5T89; -.
ProteinModelPortal; P15692; -.
SMR; P15692; -.
BioGrid; 113265; 36.
DIP; DIP-5740N; -.
IntAct; P15692; 17.
MINT; MINT-2834049; -.
STRING; 9606.ENSP00000361125; -.
BindingDB; P15692; -.
ChEMBL; CHEMBL1783; -.
DrugBank; DB05434; ABT-510.
DrugBank; DB08885; Aflibercept.
DrugBank; DB00112; Bevacizumab.
DrugBank; DB01136; Carvedilol.
DrugBank; DB06779; Dalteparin.
DrugBank; DB01120; Gliclazide.
DrugBank; DB01017; Minocycline.
DrugBank; DB03088; Pyroglutamic Acid.
DrugBank; DB01270; Ranibizumab.
DrugBank; DB03754; Tris.
DrugBank; DB05294; Vandetanib.
DrugBank; DB05890; VEGF-AS.
PhosphoSitePlus; P15692; -.
BioMuta; VEGFA; -.
DMDM; 17380528; -.
PaxDb; P15692; -.
PeptideAtlas; P15692; -.
PRIDE; P15692; -.
DNASU; 7422; -.
Ensembl; ENST00000372077; ENSP00000361148; ENSG00000112715. [P15692-9]
Ensembl; ENST00000457104; ENSP00000409911; ENSG00000112715. [P15692-10]
Ensembl; ENST00000518689; ENSP00000430829; ENSG00000112715. [P15692-3]
Ensembl; ENST00000518824; ENSP00000430002; ENSG00000112715. [P15692-8]
Ensembl; ENST00000520948; ENSP00000428321; ENSG00000112715. [P15692-2]
Ensembl; ENST00000523125; ENSP00000429008; ENSG00000112715. [P15692-5]
Ensembl; ENST00000523873; ENSP00000430479; ENSG00000112715. [P15692-1]
Ensembl; ENST00000523950; ENSP00000429643; ENSG00000112715. [P15692-4]
Ensembl; ENST00000611736; ENSP00000478570; ENSG00000112715. [P15692-14]
Ensembl; ENST00000615393; ENSP00000478034; ENSG00000112715. [P15692-12]
Ensembl; ENST00000617771; ENSP00000484284; ENSG00000112715. [P15692-15]
Ensembl; ENST00000621747; ENSP00000483241; ENSG00000112715. [P15692-11]
Ensembl; ENST00000640482; ENSP00000492800; ENSG00000112715. [P15692-17]
Ensembl; ENST00000640499; ENSP00000492413; ENSG00000112715. [P15692-13]
Ensembl; ENST00000640653; ENSP00000492199; ENSG00000112715. [P15692-16]
GeneID; 7422; -.
KEGG; hsa:7422; -.
UCSC; uc003owd.5; human. [P15692-1]
CTD; 7422; -.
DisGeNET; 7422; -.
GeneCards; VEGFA; -.
HGNC; HGNC:12680; VEGFA.
HPA; CAB005429; -.
HPA; CAB039240; -.
HPA; HPA069116; -.
MalaCards; VEGFA; -.
MIM; 192240; gene.
MIM; 603933; phenotype.
neXtProt; NX_P15692; -.
OpenTargets; ENSG00000112715; -.
PharmGKB; PA37302; -.
eggNOG; ENOG410IGCM; Eukaryota.
eggNOG; ENOG410ZWYU; LUCA.
GeneTree; ENSGT00730000110791; -.
HOVERGEN; HBG000105; -.
InParanoid; P15692; -.
KO; K05448; -.
PhylomeDB; P15692; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
Reactome; R-HSA-194313; VEGF ligand-receptor interactions.
Reactome; R-HSA-195399; VEGF binds to VEGFR leading to receptor dimerization.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SIGNOR; P15692; -.
ChiTaRS; VEGFA; human.
EvolutionaryTrace; P15692; -.
GeneWiki; Vascular_endothelial_growth_factor_A; -.
GenomeRNAi; 7422; -.
PRO; PR:P15692; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112715; -.
ExpressionAtlas; P15692; baseline and differential.
Genevisible; P15692; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; NAS:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0050840; F:extracellular matrix binding; IC:BHF-UCL.
GO; GO:0001968; F:fibronectin binding; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0038191; F:neuropilin binding; IPI:BHF-UCL.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
GO; GO:0048018; F:receptor agonist activity; IPI:BHF-UCL.
GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IPI:BHF-UCL.
GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:BHF-UCL.
GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IPI:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0048844; P:artery morphogenesis; ISS:BHF-UCL.
GO; GO:0002575; P:basophil chemotaxis; IDA:UniProtKB.
GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:BHF-UCL.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:BHF-UCL.
GO; GO:0048593; P:camera-type eye morphogenesis; ISS:BHF-UCL.
GO; GO:0048739; P:cardiac muscle fiber development; ISS:BHF-UCL.
GO; GO:0060948; P:cardiac vascular smooth muscle cell development; ISS:BHF-UCL.
GO; GO:0048469; P:cell maturation; ISS:BHF-UCL.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:BHF-UCL.
GO; GO:0071679; P:commissural neuron axon guidance; ISS:BHF-UCL.
GO; GO:0060982; P:coronary artery morphogenesis; ISS:BHF-UCL.
GO; GO:0003169; P:coronary vein morphogenesis; ISS:BHF-UCL.
GO; GO:0071542; P:dopaminergic neuron differentiation; ISS:BHF-UCL.
GO; GO:0035767; P:endothelial cell chemotaxis; IDA:BHF-UCL.
GO; GO:0030855; P:epithelial cell differentiation; ISS:BHF-UCL.
GO; GO:0042462; P:eye photoreceptor cell development; ISS:BHF-UCL.
GO; GO:0040007; P:growth; ISS:BHF-UCL.
GO; GO:0003007; P:heart morphogenesis; ISS:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; ISS:BHF-UCL.
GO; GO:0050930; P:induction of positive chemotaxis; IDA:UniProtKB.
GO; GO:0001822; P:kidney development; ISS:BHF-UCL.
GO; GO:0007595; P:lactation; ISS:BHF-UCL.
GO; GO:0030324; P:lung development; ISS:BHF-UCL.
GO; GO:0036303; P:lymph vessel morphogenesis; ISS:BHF-UCL.
GO; GO:0030225; P:macrophage differentiation; IDA:DFLAT.
GO; GO:0060749; P:mammary gland alveolus development; ISS:BHF-UCL.
GO; GO:0007498; P:mesoderm development; ISS:BHF-UCL.
GO; GO:0030224; P:monocyte differentiation; IDA:DFLAT.
GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0001541; P:ovarian follicle development; ISS:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0050918; P:positive chemotaxis; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISS:BHF-UCL.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:BHF-UCL.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0051272; P:positive regulation of cellular component movement; IDA:BHF-UCL.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; IDA:BHF-UCL.
GO; GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; IDA:BHF-UCL.
GO; GO:0002687; P:positive regulation of leukocyte migration; TAS:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IDA:UniProtKB.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:BHF-UCL.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:BHF-UCL.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:1900086; P:positive regulation of peptidyl-tyrosine autophosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:UniProtKB.
GO; GO:0090037; P:positive regulation of protein kinase C signaling; IDA:BHF-UCL.
GO; GO:1903572; P:positive regulation of protein kinase D signaling; IDA:BHF-UCL.
GO; GO:1902966; P:positive regulation of protein localization to early endosome; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0002092; P:positive regulation of receptor internalization; IDA:BHF-UCL.
GO; GO:1902336; P:positive regulation of retinal ganglion cell axon guidance; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IMP:BHF-UCL.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0043117; P:positive regulation of vascular permeability; IDA:UniProtKB.
GO; GO:0031077; P:post-embryonic camera-type eye development; ISS:BHF-UCL.
GO; GO:0060319; P:primitive erythrocyte differentiation; ISS:BHF-UCL.
GO; GO:0008360; P:regulation of cell shape; IDA:BHF-UCL.
GO; GO:0030823; P:regulation of cGMP metabolic process; IDA:MGI.
GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; ISS:BHF-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
GO; GO:0043129; P:surfactant homeostasis; ISS:BHF-UCL.
GO; GO:0035148; P:tube formation; IDA:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IDA:BHF-UCL.
GO; GO:0001570; P:vasculogenesis; TAS:UniProtKB.
GO; GO:0038190; P:VEGF-activated neuropilin signaling pathway; ISS:BHF-UCL.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.160.10; -; 1.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR023581; PD_growth_factor_CS.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR027928; VEGF_C.
Pfam; PF00341; PDGF; 1.
Pfam; PF14554; VEGF_C; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF57501; SSF57501; 1.
SUPFAM; SSF57593; SSF57593; 1.
PROSITE; PS00249; PDGF_1; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative promoter usage;
Alternative splicing; Angiogenesis; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Glycoprotein; Growth factor; Heparin-binding; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:7678805}.
CHAIN 27 232 Vascular endothelial growth factor A.
/FTId=PRO_0000023386.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
DISULFID 52 94
DISULFID 77 77 Interchain.
DISULFID 83 128
DISULFID 86 86 Interchain.
DISULFID 87 130
VAR_SEQ 1 1 M -> MTDRQTDTAPSPSYHLLPGRRRTVDAAASRGQGPEP
APGGGVEGVGARGVALKLFVQLLGCSRFGGAVVRAGEAEPS
GAARSASSGREEPQPEEGEEEEEKEEERGPQWRLGARKPGS
WTGEAAVCADSAPAARAPQALARASGRGGRVARRGAEESGP
PHSPSRRGSASRAGPGRASETM (in isoform L-
VEGF165, isoform L-VEGF121, isoform L-
VEGF189, isoform L-VEGF206, isoform 15,
isoform 16, isoform 17 and isoform 18).
{ECO:0000303|PubMed:9450968}.
/FTId=VSP_038745.
VAR_SEQ 132 226 Missing (in isoform VEGF111 and isoform
18). {ECO:0000303|Ref.16}.
/FTId=VSP_026781.
VAR_SEQ 141 182 KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGP
H -> N (in isoform 15 and isoform 17).
{ECO:0000305}.
/FTId=VSP_054111.
VAR_SEQ 141 141 K -> N (in isoform VEGF148, isoform
VEGF165, isoform VEGF165B and isoform L-
VEGF165). {ECO:0000303|PubMed:10464055,
ECO:0000303|PubMed:12124351,
ECO:0000303|PubMed:1567395,
ECO:0000303|PubMed:19054851,
ECO:0000303|PubMed:2479986,
ECO:0000303|PubMed:9450968,
ECO:0000303|Ref.11, ECO:0000303|Ref.13,
ECO:0000303|Ref.14, ECO:0000303|Ref.15}.
/FTId=VSP_004618.
VAR_SEQ 142 226 Missing (in isoform VEGF121 and isoform
L-VEGF121). {ECO:0000303|Ref.12}.
/FTId=VSP_004620.
VAR_SEQ 142 182 Missing (in isoform VEGF148, isoform
VEGF165, isoform VEGF165B and isoform L-
VEGF165). {ECO:0000303|PubMed:10464055,
ECO:0000303|PubMed:12124351,
ECO:0000303|PubMed:1567395,
ECO:0000303|PubMed:19054851,
ECO:0000303|PubMed:2479986,
ECO:0000303|PubMed:9450968,
ECO:0000303|Ref.11, ECO:0000303|Ref.13,
ECO:0000303|Ref.14, ECO:0000303|Ref.15}.
/FTId=VSP_004619.
VAR_SEQ 160 182 Missing (in isoform VEGF183 and isoform
16). {ECO:0000303|PubMed:10067980,
ECO:0000303|PubMed:9878851}.
/FTId=VSP_004621.
VAR_SEQ 166 226 Missing (in isoform VEGF145).
{ECO:0000303|PubMed:9054410}.
/FTId=VSP_004623.
VAR_SEQ 166 182 Missing (in isoform VEGF189 and isoform
L-VEGF189). {ECO:0000303|PubMed:2479986,
ECO:0000303|PubMed:2479987}.
/FTId=VSP_004622.
VAR_SEQ 215 215 A -> M (in isoform VEGF148 and isoform
17). {ECO:0000303|PubMed:10464055}.
/FTId=VSP_004624.
VAR_SEQ 216 232 Missing (in isoform VEGF148 and isoform
17). {ECO:0000303|PubMed:10464055}.
/FTId=VSP_004625.
VAR_SEQ 227 232 CDKPRR -> SLTRKD (in isoform VEGF165B and
isoform 15).
{ECO:0000303|PubMed:12124351}.
/FTId=VSP_014783.
CONFLICT 87 87 C -> S (in Ref. 8; AAC63143).
{ECO:0000305}.
CONFLICT 210 210 D -> H (in Ref. 8; AAC63143).
{ECO:0000305}.
HELIX 43 50 {ECO:0000244|PDB:1MKK}.
STRAND 51 60 {ECO:0000244|PDB:1MKK}.
HELIX 61 64 {ECO:0000244|PDB:1MKK}.
HELIX 66 68 {ECO:0000244|PDB:1MKK}.
STRAND 71 84 {ECO:0000244|PDB:1MKK}.
STRAND 93 109 {ECO:0000244|PDB:1MKK}.
TURN 111 113 {ECO:0000244|PDB:4GLN}.
STRAND 116 131 {ECO:0000244|PDB:1MKK}.
STRAND 189 191 {ECO:0000244|PDB:4DEQ}.
STRAND 194 197 {ECO:0000244|PDB:4DEQ}.
TURN 199 201 {ECO:0000244|PDB:4DEQ}.
STRAND 204 208 {ECO:0000244|PDB:4DEQ}.
HELIX 210 214 {ECO:0000244|PDB:4DEQ}.
TURN 215 217 {ECO:0000244|PDB:4DEQ}.
STRAND 219 221 {ECO:0000244|PDB:1KMX}.
TURN 222 224 {ECO:0000244|PDB:4DEQ}.
STRAND 226 228 {ECO:0000244|PDB:1KMX}.
SEQUENCE 232 AA; 27042 MW; FB49F364446F4D01 CRC64;
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD
IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM
SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVYVGAR CCLMPWSLPG
PHPCGPCSER RKHLFVQDPQ TCKCSCKNTD SRCKARQLEL NERTCRCDKP RR


Related products :

Catalog number Product name Quantity
20-271-80050 Vascular Endothelial Cell Growth Factor - Mouse Anti Human Vascular Endothelial Cell Growth Factor; VEGF-A; Vascular permeability factor; VPF Monoclonal 0.5 mg
20-271-80050 Vascular Endothelial Cell Growth Factor - Mouse Anti Human Vascular Endothelial Cell Growth Factor; VEGF-A; Vascular permeability factor; VPF Monoclonal 1 mg
U0143h CLIA Homo sapiens,Human,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
E0143h ELISA kit Homo sapiens,Human,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
E0143h ELISA Homo sapiens,Human,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
U0143b CLIA Bos taurus,Bovine,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
E0143r ELISA kit Rat,Rattus norvegicus,Vascular endothelial growth factor A,Vascular permeability factor,Vegf,Vegfa,VEGF-A,VPF 96T
U0143r CLIA Rat,Rattus norvegicus,Vascular endothelial growth factor A,Vascular permeability factor,Vegf,Vegfa,VEGF-A,VPF 96T
E0143m ELISA kit Mouse,Mus musculus,Vascular endothelial growth factor A,Vascular permeability factor,Vegf,Vegfa,VEGF-A,VPF 96T
U0143m CLIA Mouse,Mus musculus,Vascular endothelial growth factor A,Vascular permeability factor,Vegf,Vegfa,VEGF-A,VPF 96T
E0143b ELISA kit Bos taurus,Bovine,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
E0143b ELISA Bos taurus,Bovine,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
E0143m ELISA Mouse,Mus musculus,Vascular endothelial growth factor A,Vascular permeability factor,Vegf,Vegfa,VEGF-A,VPF 96T
E0143r ELISA Rat,Rattus norvegicus,Vascular endothelial growth factor A,Vascular permeability factor,Vegf,Vegfa,VEGF-A,VPF 96T
E0143p ELISA Pig,Sus scrofa,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
E0143p ELISA kit Pig,Sus scrofa,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
U0143p CLIA Pig,Sus scrofa,Vascular endothelial growth factor A,Vascular permeability factor,VEGF,VEGFA,VEGF-A,VPF 96T
10-663-45071 Vascular Endothelial Growth Factor-121 glycosylated (VEGF-121) Human - VEGF-A; Vascular permeability factor; VPF N_A 0.002 mg
10-663-45071 Vascular Endothelial Growth Factor-121 glycosylated (VEGF-121) Human - VEGF-A; Vascular permeability factor; VPF N_A 0.01 mg
10-663-45174 Vascular Endothelial Growth Factor variant (VEGF-121) Human - VEGF-A; Vascular permeability factor; VPF N_A 0.002 mg
10-663-45174 Vascular Endothelial Growth Factor variant (VEGF-121) Human - VEGF-A; Vascular permeability factor; VPF N_A 1 mg
10-663-45174 Vascular Endothelial Growth Factor variant (VEGF-121) Human - VEGF-A; Vascular permeability factor; VPF N_A 0.01 mg
10-663-45071 Vascular Endothelial Growth Factor-121 glycosylated (VEGF-121) Human - VEGF-A; Vascular permeability factor; VPF N_A 1 mg
20-663-48024 Vascular Endothelial Cell Growth Factor (mAHuVEGF) - Mouse Anti-Human Vascular Endothelial Cell Growth Factor (mAHuVEGF); VEGF-A; Vascular permeability factor; VPF Monoclonal 1 mg
20-663-48024 Vascular Endothelial Cell Growth Factor (mAHuVEGF) - Mouse Anti-Human Vascular Endothelial Cell Growth Factor (mAHuVEGF); VEGF-A; Vascular permeability factor; VPF Monoclonal 0.5 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur