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Fibroblast growth factor 2 (FGF-2) (Basic fibroblast growth factor) (bFGF) (Heparin-binding growth factor 2) (HBGF-2)

 FGF2_HUMAN              Reviewed;         288 AA.
P09038; A4LBB8; O00527; P78443; Q16443; Q5PY50; Q7KZ11; Q7KZ72;
Q9UC54; Q9UCS5; Q9UCS6;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
13-OCT-2009, sequence version 3.
20-JUN-2018, entry version 219.
RecName: Full=Fibroblast growth factor 2;
Short=FGF-2;
AltName: Full=Basic fibroblast growth factor;
Short=bFGF;
AltName: Full=Heparin-binding growth factor 2;
Short=HBGF-2;
Flags: Precursor;
Name=FGF2; Synonyms=FGFB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3472745;
Abraham J.A., Whang J.L., Tumolo A., Mergia A., Fiddes J.C.;
"Human basic fibroblast growth factor: nucleotide sequence, genomic
organization, and expression in mammalian cells.";
Cold Spring Harb. Symp. Quant. Biol. 51:657-668(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=3780670;
Abraham J.A., Whang J.L., Tumolo A., Mergia A., Friedman J.,
Gospodarowicz D., Fiddes J.C.;
"Human basic fibroblast growth factor: nucleotide sequence and genomic
organization.";
EMBO J. 5:2523-2528(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), PROTEIN SEQUENCE OF
126-145 (ISOFORMS 1/2/4), AND ALTERNATIVE INITIATION.
TISSUE=Hepatoma;
PubMed=2538817; DOI=10.1073/pnas.86.6.1836;
Prats H., Kaghad M., Prats A.C., Klagsbrun M., Lelias J.M.,
Liauzun P., Chalon P., Tauber J.P., Amalric F., Smith J.A., Caput D.;
"High molecular mass forms of basic fibroblast growth factor are
initiated by alternative CUG codons.";
Proc. Natl. Acad. Sci. U.S.A. 86:1836-1840(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
PubMed=1785797; DOI=10.1111/j.1749-6632.1991.tb49022.x;
Florkiewicz R.Z., Shibata F., Barankiewicz T., Baird A.,
Gonzalez A.M., Florkiewicz E., Shah N.;
"Basic fibroblast growth factor gene expression.";
Ann. N. Y. Acad. Sci. 638:109-126(1991).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
TISSUE=Blood;
Handschug K., Archoukieh E., Glaeser C.;
"Mutations in the 5' untranslated region of the FGF-2 gene.";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-288 (ISOFORM 1).
PubMed=2435575; DOI=10.1016/0014-5793(87)81489-8;
Kurokawa T., Sasada R., Iwane M., Igarashi K.;
"Cloning and expression of cDNA encoding human basic fibroblast growth
factor.";
FEBS Lett. 213:189-194(1987).
[11]
PROTEIN SEQUENCE OF 94-107 AND 162-173, FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Hepatoma;
PubMed=1721615; DOI=10.1111/j.1349-7006.1991.tb01791.x;
Shimoyama Y., Gotoh M., Ino Y., Sakamoto M., Kato K., Hirohashi S.;
"Characterization of high-molecular-mass forms of basic fibroblast
growth factor produced by hepatocellular carcinoma cells: possible
involvement of basic fibroblast growth factor in
hepatocarcinogenesis.";
Jpn. J. Cancer Res. 82:1263-1270(1991).
[12]
PROTEIN SEQUENCE OF 125-140 (ISOFORMS 1/2/4).
PubMed=8564983;
Izbicka E., Dunstan C., Esparza J., Jacobs C., Sabatini M.,
Mundy G.R.;
"Human amniotic tumor that induces new bone formation in vivo produces
growth-regulatory activity in vitro for osteoblasts identified as an
extended form of basic fibroblast growth factor.";
Cancer Res. 56:633-636(1996).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 132-288 (ISOFORMS 1/2/4), AND PROTEIN
SEQUENCE OF 132-148; 153-160; 165-247; 252-261 AND 267-288 (ISOFORMS
2/4).
TISSUE=Hepatoma, and Placenta;
PubMed=3579930; DOI=10.1016/S0006-291X(87)80001-3;
Sommer A., Brewer M.T., Thompson R.C., Moscatelli D., Presta M.,
Rifkin D.B.;
"A form of human basic fibroblast growth factor with an extended amino
terminus.";
Biochem. Biophys. Res. Commun. 144:543-550(1987).
[14]
PROTEIN SEQUENCE OF 135-155 (ISOFORMS 1/2/3/4).
PubMed=2435284; DOI=10.1016/0006-291X(87)91471-9;
Story M.T., Esch F., Shimasaki S., Sasse J., Jacobs S.C., Lawson R.K.;
"Amino-terminal sequence of a large form of basic fibroblast growth
factor isolated from human benign prostatic hyperplastic tissue.";
Biochem. Biophys. Res. Commun. 142:702-709(1987).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 143-288 (ISOFORMS 1/2/3/4).
Zhang H.J., Zhang S.M., Zhuang H.;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[16]
PROTEIN SEQUENCE OF 143-172 (ISOFORMS 1/2/3/4), AND FUNCTION.
PubMed=3964259; DOI=10.1016/0006-291X(86)90028-8;
Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.;
"Human brain-derived acidic and basic fibroblast growth factors: amino
terminal sequences and specific mitogenic activities.";
Biochem. Biophys. Res. Commun. 135:541-548(1986).
[17]
PROTEIN SEQUENCE OF 143-168 (ISOFORMS 1/2/3/4), AND FUNCTION.
PubMed=3732516; DOI=10.1016/0014-5793(86)80812-2;
Gautschi P., Frater-Schroeder M., Boehlen P.;
"Partial molecular characterization of endothelial cell mitogens from
human brain: acidic and basic fibroblast growth factors.";
FEBS Lett. 204:203-207(1986).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 173-260 (ISOFORMS 1/2/3/4), AND TISSUE
SPECIFICITY.
PubMed=1417798; DOI=10.1016/0006-291X(92)90434-M;
Watson R., Anthony F., Pickett M., Lambden P., Masson G.M.,
Thomas E.J.;
"Reverse transcription with nested polymerase chain reaction shows
expression of basic fibroblast growth factor transcripts in human
granulosa and cumulus cells from in vitro fertilisation patients.";
Biochem. Biophys. Res. Commun. 187:1227-1231(1992).
[19]
IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF1.
PubMed=1885605;
Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.;
"Characterization and molecular cloning of a putative binding protein
for heparin-binding growth factors.";
J. Biol. Chem. 266:16778-16785(1991).
[20]
FUNCTION, AND INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4.
PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
Coulier F., Gao G., Goldfarb M.;
"Receptor specificity of the fibroblast growth factor family.";
J. Biol. Chem. 271:15292-15297(1996).
[21]
INTERACTION WITH CSPG4.
PubMed=10358027; DOI=10.1074/jbc.274.24.16831;
Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.;
"High-affinity binding of basic fibroblast growth factor and platelet-
derived growth factor-AA to the core protein of the NG2
proteoglycan.";
J. Biol. Chem. 274:16831-16837(1999).
[22]
INTERACTION WITH FGFBP1.
PubMed=11509569; DOI=10.1074/jbc.M104933200;
Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K.,
Karavanov A., Wellstein A.;
"Enhancement of fibroblast growth factor (FGF) activity by an FGF-
binding protein.";
J. Biol. Chem. 276:40247-40253(2001).
[23]
INTERACTION WITH FGF1.
PubMed=11964394; DOI=10.1074/jbc.M112193200;
Skjerpen C.S., Wesche J., Olsnes S.;
"Identification of ribosome-binding protein p34 as an intracellular
protein that binds acidic fibroblast growth factor.";
J. Biol. Chem. 277:23864-23871(2002).
[24]
INTERACTION WITH FGFBP1.
PubMed=16257968; DOI=10.1074/jbc.M510754200;
Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S.,
Ueda Y., Tomita Y., Riegel A.T., Wellstein A.;
"Identification of the fibroblast growth factor (FGF)-interacting
domain in a secreted FGF-binding protein by phage display.";
J. Biol. Chem. 281:1137-1144(2006).
[25]
INTERACTION WITH FGFBP3.
PubMed=18669637; DOI=10.1074/jbc.M802144200;
Zhang W., Chen Y., Swift M.R., Tassi E., Stylianou D.C., Gibby K.A.,
Riegel A.T., Wellstein A.;
"Effect of FGF-binding protein 3 on vascular permeability.";
J. Biol. Chem. 283:28329-28337(2008).
[26]
PHOSPHORYLATION AT TYR-215, INTERACTION WITH TEC, AND SUBCELLULAR
LOCATION.
PubMed=20230531; DOI=10.1111/j.1600-0854.2010.01059.x;
Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H.,
Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.;
"Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is
essential for unconventional secretion.";
Traffic 11:813-826(2010).
[27]
REVIEW.
PubMed=15863030; DOI=10.1016/j.cytogfr.2005.01.001;
Eswarakumar V.P., Lax I., Schlessinger J.;
"Cellular signaling by fibroblast growth factor receptors.";
Cytokine Growth Factor Rev. 16:139-149(2005).
[28]
REVIEW.
PubMed=20094046; DOI=10.1038/nrc2780;
Turner N., Grose R.;
"Fibroblast growth factor signalling: from development to cancer.";
Nat. Rev. Cancer 10:116-129(2010).
[29]
SUBCELLULAR LOCATION.
PubMed=22321063; DOI=10.1111/j.1600-0854.2012.01341.x;
Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y.,
Walchli S., Olsnes S., Wiedlocha A.;
"Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and
the importins Kpnalpha1 and Kpnbeta1.";
Traffic 13:650-664(2012).
[30]
FUNCTION.
PubMed=23469107; DOI=10.1371/journal.pone.0057927;
Mori S., Tran V., Nishikawa K., Kaneda T., Hamada Y., Kawaguchi N.,
Fujita M., Saegusa J., Takada Y.K., Matsuura N., Zhao M., Takada Y.;
"A dominant-negative FGF1 mutant (the R50E mutant) suppresses
tumorigenesis and angiogenesis.";
PLoS ONE 8:E57927-E57927(2013).
[31]
ERRATUM.
Mori S., Tran V., Nishikawa K., Kaneda T., Hamada Y., Kawaguchi N.,
Fujita M., Saegusa J., Takada Y.K., Matsuura N., Zhao M., Takada Y.;
PLoS ONE 8:E91599-E91599(2013).
[32]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-228, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[33]
FUNCTION, INTERACTION WITH INTEGRIN ITGAV:ITGB3, SITES IMPORTANT FOR
INTEGRIN BINDING, AND MUTAGENESIS OF ARG-181; ARG-186; LYS-188;
261-LYS-ARG-262 AND LYS-267.
PubMed=28302677; DOI=10.1042/BSR20170173;
Mori S., Hatori N., Kawaguchi N., Hamada Y., Shih T.C., Wu C.Y.,
Lam K.S., Matsuura N., Yamamoto H., Takada Y.K., Takada Y.;
"The integrin-binding defective FGF2 mutants potently suppress FGF2
signalling and angiogenesis.";
Biosci. Rep. 37:0-0(2017).
[34]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
PubMed=1769963;
Ago H., Kitagawa Y., Fujishima A., Matsuura Y., Katsube Y.;
"Crystal structure of basic fibroblast growth factor at 1.6-A
resolution.";
J. Biochem. 110:360-363(1991).
[35]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 143-288.
PubMed=1707542; DOI=10.1073/pnas.88.8.3441;
Eriksson A.E., Cousens L.S., Weaver L.H., Matthews B.W.;
"Three-dimensional structure of human basic fibroblast growth
factor.";
Proc. Natl. Acad. Sci. U.S.A. 88:3441-3445(1991).
[36]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 143-288.
PubMed=1849658; DOI=10.1073/pnas.88.8.3446;
Zhang J., Cousens L.S., Barr P.J., Sprang S.R.;
"Three-dimensional structure of human basic fibroblast growth factor,
a structural homolog of interleukin 1 beta.";
Proc. Natl. Acad. Sci. U.S.A. 88:3446-3450(1991).
[37]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 135-288.
PubMed=1702556; DOI=10.1126/science.1702556;
Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T.,
Hsu B.T., Rees D.C.;
"Three-dimensional structures of acidic and basic fibroblast growth
factors.";
Science 251:90-93(1991).
[38]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
PubMed=7691311; DOI=10.1002/pro.5560020810;
Eriksson A.E., Cousens L.S., Matthews B.W.;
"Refinement of the structure of human basic fibroblast growth factor
at 1.6-A resolution and analysis of presumed heparin binding sites by
selenate substitution.";
Protein Sci. 2:1274-1284(1993).
[39]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 134-288 IN COMPLEX WITH
FGFR2.
PubMed=11390973; DOI=10.1073/pnas.121183798;
Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M.,
Mohammadi M.;
"Structural basis for fibroblast growth factor receptor 2 activation
in Apert syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001).
[40]
STRUCTURE BY NMR OF 134-288.
PubMed=8885834; DOI=10.1021/bi961260p;
Moy F.J., Seddon A.P., Boehlen P., Powers R.;
"High-resolution solution structure of basic fibroblast growth factor
determined by multidimensional heteronuclear magnetic resonance
spectroscopy.";
Biochemistry 35:13552-13561(1996).
-!- FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4
(PubMed:8663044). Also acts as an integrin ligand which is
required for FGF2 signaling (PubMed:28302677). Binds to integrin
ITGAV:ITGB3 (PubMed:28302677). Plays an important role in the
regulation of cell survival, cell division, cell differentiation
and cell migration (PubMed:8663044, PubMed:28302677). Functions as
a potent mitogen in vitro (PubMed:3732516, PubMed:3964259). Can
induce angiogenesis (PubMed:23469107, PubMed:28302677).
{ECO:0000269|PubMed:1721615, ECO:0000269|PubMed:23469107,
ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:3732516,
ECO:0000269|PubMed:3964259, ECO:0000269|PubMed:8663044}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Retains almost half of its activity after treatment at pH 2.0
for 3 hours at 20 degrees Celsius. {ECO:0000269|PubMed:1721615};
Temperature dependence:
Inactivated after 3 minutes at 60 degrees Celsius or 1 minute at
80 degrees Celsius. {ECO:0000269|PubMed:1721615};
-!- SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3
and FGFR4. Affinity between fibroblast growth factors (FGFs) and
their receptors is increased by heparan sulfate glycosaminoglycans
that function as coreceptors. Interacts with CSPG4, FGFBP1 and
TEC. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with
FGFBP3 (PubMed:18669637). Interacts with integrin ITGAV:ITGB3; the
interaction is required for FGF2 signaling (PubMed:28302677).
Interacts with SNORC (via the extracellular domain) (By
similarity). {ECO:0000250|UniProtKB:P15655,
ECO:0000269|PubMed:10358027, ECO:0000269|PubMed:11390973,
ECO:0000269|PubMed:11509569, ECO:0000269|PubMed:11964394,
ECO:0000269|PubMed:16257968, ECO:0000269|PubMed:18669637,
ECO:0000269|PubMed:1885605, ECO:0000269|PubMed:20230531,
ECO:0000269|PubMed:28302677, ECO:0000269|PubMed:8663044}.
-!- INTERACTION:
P29466:CASP1; NbExp=2; IntAct=EBI-977447, EBI-516667;
Q14512:FGFBP1; NbExp=3; IntAct=EBI-977447, EBI-953742;
P11362:FGFR1; NbExp=5; IntAct=EBI-977447, EBI-1028277;
P11362-14:FGFR1; NbExp=2; IntAct=EBI-977447, EBI-6622185;
P11362-7:FGFR1; NbExp=2; IntAct=EBI-977447, EBI-15609945;
P21802:FGFR2; NbExp=3; IntAct=EBI-977447, EBI-1028658;
P26022:PTX3; NbExp=16; IntAct=EBI-977447, EBI-11574553;
-!- SUBCELLULAR LOCATION: Secreted. Nucleus. Note=Exported from cells
by an endoplasmic reticulum (ER)/Golgi-independent mechanism.
Unconventional secretion of FGF2 occurs by direct translocation
across the plasma membrane. Binding of exogenous FGF2 to FGFR
facilitates endocytosis followed by translocation of FGF2 across
endosomal membrane into the cytosol. Nuclear import from the
cytosol requires the classical nuclear import machinery, involving
proteins KPNA1 and KPNB1, as well as CEP57.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=4;
Name=1;
IsoId=P09038-4; Sequence=Displayed;
Note=Starts at an alternative CUG codon.;
Name=2;
IsoId=P09038-1; Sequence=VSP_038236, VSP_038237;
Note=Starts at an alternative CUG codon.;
Name=3;
IsoId=P09038-2; Sequence=VSP_037383;
Name=4;
IsoId=P09038-3; Sequence=VSP_037384, VSP_037385;
Note=Starts at an alternative CUG codon.;
-!- TISSUE SPECIFICITY: Expressed in granulosa and cumulus cells.
Expressed in hepatocellular carcinoma cells, but not in non-
cancerous liver tissue. {ECO:0000269|PubMed:1417798,
ECO:0000269|PubMed:1721615}.
-!- PTM: Phosphorylation at Tyr-215 regulates FGF2 unconventional
secretion. {ECO:0000269|PubMed:20230531}.
-!- PTM: Several N-termini starting at positions 94, 125, 126, 132,
143 and 162 have been identified by direct sequencing.
-!- MISCELLANEOUS: This protein binds heparin more strongly than does
aFGF.
-!- SIMILARITY: Belongs to the heparin-binding growth factors family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA52448.1; Type=Frameshift; Positions=25, 82, 98, 133; Evidence={ECO:0000305};
Sequence=AAB21432.2; Type=Frameshift; Positions=25; Evidence={ECO:0000305};
Sequence=AAB21432.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=ABO43041.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=ABO43041.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=CAA28027.1; Type=Frameshift; Positions=25, 102; Evidence={ECO:0000305};
Sequence=CAA28027.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=CAA73868.1; Type=Frameshift; Positions=25; Evidence={ECO:0000305};
Sequence=CAA73868.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=EAX05222.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=EAX05222.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgf2/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FGF2ID511ch4q27.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X04431; CAA28027.1; ALT_SEQ; Genomic_DNA.
EMBL; X04432; CAA28028.1; -; Genomic_DNA.
EMBL; X04433; CAA28029.1; -; Genomic_DNA.
EMBL; J04513; AAA52531.1; -; mRNA.
EMBL; J04513; AAA52532.1; -; mRNA.
EMBL; J04513; AAA52533.1; -; mRNA.
EMBL; AB451321; BAG70135.1; -; mRNA.
EMBL; AB451450; BAG70264.1; -; mRNA.
EMBL; EF506888; ABO43041.1; ALT_SEQ; Genomic_DNA.
EMBL; AC021205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX05222.1; ALT_SEQ; Genomic_DNA.
EMBL; S81809; AAB21432.2; ALT_SEQ; Genomic_DNA.
EMBL; Y13468; CAA73868.1; ALT_SEQ; Genomic_DNA.
EMBL; M27968; AAA52448.1; ALT_FRAME; mRNA.
EMBL; M17599; AAA52534.1; -; mRNA.
EMBL; AY820133; AAV70487.1; -; mRNA.
EMBL; S47380; AAD13853.1; -; mRNA.
CCDS; CCDS34059.1; -. [P09038-4]
PIR; A32398; A32398.
RefSeq; NP_001997.5; NM_002006.4. [P09038-4]
UniGene; Hs.284244; -.
PDB; 1BAS; X-ray; 1.90 A; A=135-288.
PDB; 1BFB; X-ray; 1.90 A; A=142-288.
PDB; 1BFC; X-ray; 2.20 A; A=142-288.
PDB; 1BFF; X-ray; 2.00 A; A=160-288.
PDB; 1BFG; X-ray; 1.60 A; A=143-288.
PDB; 1BLA; NMR; -; A=134-288.
PDB; 1BLD; NMR; -; A=134-288.
PDB; 1CVS; X-ray; 2.80 A; A/B=157-288.
PDB; 1EV2; X-ray; 2.20 A; A/B/C/D=157-288.
PDB; 1FGA; X-ray; 2.20 A; A=143-288.
PDB; 1FQ9; X-ray; 3.00 A; A/B=157-288.
PDB; 1II4; X-ray; 2.70 A; A/B/C/D=134-288.
PDB; 1IIL; X-ray; 2.30 A; A/B/C/D=134-288.
PDB; 2BFH; X-ray; 2.50 A; A=161-288.
PDB; 2FGF; X-ray; 1.77 A; A=143-288.
PDB; 2M49; NMR; -; A/C=161-286.
PDB; 4FGF; X-ray; 1.60 A; A=143-288.
PDB; 4OEE; X-ray; 1.50 A; A=134-288.
PDB; 4OEF; X-ray; 1.80 A; A=134-288.
PDB; 4OEG; X-ray; 1.60 A; A=134-288.
PDB; 5X1O; X-ray; 1.90 A; A/B=143-288.
PDBsum; 1BAS; -.
PDBsum; 1BFB; -.
PDBsum; 1BFC; -.
PDBsum; 1BFF; -.
PDBsum; 1BFG; -.
PDBsum; 1BLA; -.
PDBsum; 1BLD; -.
PDBsum; 1CVS; -.
PDBsum; 1EV2; -.
PDBsum; 1FGA; -.
PDBsum; 1FQ9; -.
PDBsum; 1II4; -.
PDBsum; 1IIL; -.
PDBsum; 2BFH; -.
PDBsum; 2FGF; -.
PDBsum; 2M49; -.
PDBsum; 4FGF; -.
PDBsum; 4OEE; -.
PDBsum; 4OEF; -.
PDBsum; 4OEG; -.
PDBsum; 5X1O; -.
ProteinModelPortal; P09038; -.
SMR; P09038; -.
BioGrid; 108538; 27.
CORUM; P09038; -.
DIP; DIP-4012N; -.
IntAct; P09038; 14.
MINT; P09038; -.
STRING; 9606.ENSP00000264498; -.
BindingDB; P09038; -.
ChEMBL; CHEMBL3107; -.
DrugBank; DB05434; ABT-510.
DrugBank; DB00686; Pentosan Polysulfate.
DrugBank; DB00877; Sirolimus.
DrugBank; DB00364; Sucralfate.
TCDB; 1.A.108.1.1; the fibroblast growth factor 2 (fgf2) family.
iPTMnet; P09038; -.
PhosphoSitePlus; P09038; -.
BioMuta; FGF2; -.
DMDM; 261260095; -.
EPD; P09038; -.
PaxDb; P09038; -.
PeptideAtlas; P09038; -.
PRIDE; P09038; -.
ProteomicsDB; 52187; -.
ProteomicsDB; 52188; -. [P09038-1]
ProteomicsDB; 52189; -. [P09038-2]
ProteomicsDB; 52190; -. [P09038-3]
DNASU; 2247; -.
Ensembl; ENST00000608478; ENSP00000477134; ENSG00000138685. [P09038-2]
Ensembl; ENST00000614010; ENSP00000478620; ENSG00000138685. [P09038-4]
Ensembl; ENST00000644866; ENSP00000494222; ENSG00000138685. [P09038-2]
GeneID; 2247; -.
KEGG; hsa:2247; -.
UCSC; uc062zki.1; human. [P09038-4]
CTD; 2247; -.
DisGeNET; 2247; -.
EuPathDB; HostDB:ENSG00000138685.12; -.
GeneCards; FGF2; -.
HGNC; HGNC:3676; FGF2.
HPA; CAB000125; -.
MIM; 134920; gene.
neXtProt; NX_P09038; -.
OpenTargets; ENSG00000138685; -.
PharmGKB; PA28115; -.
eggNOG; KOG3885; Eukaryota.
eggNOG; ENOG4111IPH; LUCA.
GeneTree; ENSGT00730000110923; -.
HOVERGEN; HBG107917; -.
InParanoid; P09038; -.
KO; K18497; -.
PhylomeDB; P09038; -.
TreeFam; TF317805; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1839122; Signaling by activated point mutants of FGFR1.
Reactome; R-HSA-1839130; Signaling by activated point mutants of FGFR3.
Reactome; R-HSA-190322; FGFR4 ligand binding and activation.
Reactome; R-HSA-190370; FGFR1b ligand binding and activation.
Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
Reactome; R-HSA-190373; FGFR1c ligand binding and activation.
Reactome; R-HSA-190375; FGFR2c ligand binding and activation.
Reactome; R-HSA-190377; FGFR2b ligand binding and activation.
Reactome; R-HSA-2033514; FGFR3 mutant receptor activation.
Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-5654219; Phospholipase C-mediated cascade: FGFR1.
Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
Reactome; R-HSA-5654227; Phospholipase C-mediated cascade, FGFR3.
Reactome; R-HSA-5654228; Phospholipase C-mediated cascade, FGFR4.
Reactome; R-HSA-5654687; Downstream signaling of activated FGFR1.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5658623; FGFRL1 modulation of FGFR1 signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
SignaLink; P09038; -.
SIGNOR; P09038; -.
ChiTaRS; FGF2; human.
EvolutionaryTrace; P09038; -.
GeneWiki; Basic_fibroblast_growth_factor; -.
GenomeRNAi; 2247; -.
PRO; PR:P09038; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138685; -.
CleanEx; HS_FGF2; -.
ExpressionAtlas; P09038; baseline and differential.
Genevisible; P09038; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:MGI.
GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0090722; F:receptor-receptor interaction; IDA:ParkinsonsUK-UCL.
GO; GO:0000187; P:activation of MAPK activity; TAS:ProtInc.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:UniProtKB.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0060591; P:chondroblast differentiation; IDA:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0048598; P:embryonic morphogenesis; TAS:DFLAT.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0014843; P:growth factor dependent regulation of skeletal muscle satellite cell proliferation; IMP:AgBase.
GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:DFLAT.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0060548; P:negative regulation of cell death; IDA:UniProtKB.
GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:UniProtKB.
GO; GO:0061045; P:negative regulation of wound healing; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:DFLAT.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0042660; P:positive regulation of cell fate specification; IDA:MGI.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; IDA:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:DFLAT.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IDA:DFLAT.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IGI:BHF-UCL.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IGI:BHF-UCL.
GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
GO; GO:0045765; P:regulation of angiogenesis; TAS:DFLAT.
GO; GO:2000544; P:regulation of endothelial cell chemotaxis to fibroblast growth factor; IDA:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:DFLAT.
GO; GO:0007165; P:signal transduction; NAS:ProtInc.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0072089; P:stem cell proliferation; NAS:ParkinsonsUK-UCL.
GO; GO:0042060; P:wound healing; IDA:UniProtKB.
CDD; cd00058; FGF; 1.
InterPro; IPR028223; FGF2.
InterPro; IPR002209; Fibroblast_GF_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR11486; PTHR11486; 1.
PANTHER; PTHR11486:SF83; PTHR11486:SF83; 1.
Pfam; PF00167; FGF; 1.
PRINTS; PR00263; HBGFFGF.
SMART; SM00442; FGF; 1.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00247; HBGF_FGF; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Angiogenesis; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Growth factor; Heparin-binding; Isopeptide bond; Methylation; Mitogen;
Nucleus; Phosphoprotein; Reference proteome; Secreted;
Ubl conjugation.
PROPEP 1 142 Or 93, or 124, or 125, or 131, or 161.
/FTId=PRO_0000008932.
CHAIN 143 288 Fibroblast growth factor 2.
/FTId=PRO_0000008933.
REGION 261 277 Heparin-binding. {ECO:0000250}.
MOTIF 179 181 Cell attachment site; atypical.
{ECO:0000255}.
MOTIF 221 223 Cell attachment site; atypical.
{ECO:0000255}.
BINDING 169 169 Heparin. {ECO:0000250}.
SITE 261 261 Important for interaction with integrin.
{ECO:0000269|PubMed:28302677}.
SITE 262 262 Important for interaction with integrin.
{ECO:0000269|PubMed:28302677}.
SITE 267 267 Important for interaction with integrin.
{ECO:0000269|PubMed:28302677}.
MOD_RES 108 108 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q60487}.
MOD_RES 108 108 Symmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q60487}.
MOD_RES 110 110 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q60487}.
MOD_RES 110 110 Symmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q60487}.
MOD_RES 112 112 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q60487}.
MOD_RES 112 112 Symmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q60487}.
MOD_RES 215 215 Phosphotyrosine; by TEC.
{ECO:0000269|PubMed:20230531}.
CROSSLNK 228 228 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 1 133 Missing (in isoform 3).
{ECO:0000303|PubMed:19054851,
ECO:0000303|PubMed:2538817}.
/FTId=VSP_037383.
VAR_SEQ 1 92 Missing (in isoform 4).
{ECO:0000303|PubMed:2538817}.
/FTId=VSP_037384.
VAR_SEQ 1 78 Missing (in isoform 2).
{ECO:0000303|PubMed:2538817}.
/FTId=VSP_038236.
VAR_SEQ 79 79 L -> M (in isoform 2).
{ECO:0000303|PubMed:2538817}.
/FTId=VSP_038237.
VAR_SEQ 93 93 L -> M (in isoform 4).
{ECO:0000303|PubMed:2538817}.
/FTId=VSP_037385.
MUTAGEN 181 181 R->E: No effect on integrin binding.
{ECO:0000269|PubMed:28302677}.
MUTAGEN 186 186 R->E: No effect on integrin binding.
{ECO:0000269|PubMed:28302677}.
MUTAGEN 188 188 K->E: No effect on integrin binding.
{ECO:0000269|PubMed:28302677}.
MUTAGEN 261 262 KR->EE: Abolishes binding to integrin
ITGAV:ITGB3 and suppresses FGF2 signaling
with loss of ERK1/2 activation and
reduced ability to induce DNA synthesis,
cell migration and angiogenesis. Acts as
a potent antagonist of FGF2-mediated
angiogenesis.
{ECO:0000269|PubMed:28302677}.
MUTAGEN 267 267 K->E: Reduces binding to integrin
ITGAV:ITGB3 and suppresses FGF2 signaling
with reduced ERK1/2 activation and
reduced ability to induce DNA synthesis,
cell migration and angiogenesis. Acts as
a potent antagonist of FGF2-mediated
angiogenesis.
{ECO:0000269|PubMed:28302677}.
CONFLICT 25 25 G -> R (in Ref. 10; AAA52448).
{ECO:0000305}.
CONFLICT 50 50 H -> Q (in Ref. 10; AAA52448).
{ECO:0000305}.
CONFLICT 59 59 A -> R (in Ref. 10; AAA52448).
{ECO:0000305}.
STRAND 136 139 {ECO:0000244|PDB:1BLA}.
STRAND 151 153 {ECO:0000244|PDB:1BLA}.
HELIX 156 160 {ECO:0000244|PDB:4OEE}.
STRAND 163 167 {ECO:0000244|PDB:4OEE}.
TURN 168 170 {ECO:0000244|PDB:4OEE}.
STRAND 173 176 {ECO:0000244|PDB:4OEE}.
STRAND 182 186 {ECO:0000244|PDB:4OEE}.
HELIX 191 193 {ECO:0000244|PDB:1BFG}.
STRAND 195 201 {ECO:0000244|PDB:4OEE}.
STRAND 204 209 {ECO:0000244|PDB:4OEE}.
TURN 210 213 {ECO:0000244|PDB:4OEE}.
STRAND 214 218 {ECO:0000244|PDB:4OEE}.
STRAND 220 222 {ECO:0000244|PDB:1BLA}.
STRAND 224 229 {ECO:0000244|PDB:4OEE}.
HELIX 232 234 {ECO:0000244|PDB:4OEE}.
STRAND 236 240 {ECO:0000244|PDB:4OEE}.
HELIX 242 244 {ECO:0000244|PDB:2FGF}.
STRAND 246 253 {ECO:0000244|PDB:4OEE}.
STRAND 264 266 {ECO:0000244|PDB:4OEE}.
HELIX 269 271 {ECO:0000244|PDB:4OEE}.
HELIX 277 279 {ECO:0000244|PDB:4OEE}.
STRAND 281 284 {ECO:0000244|PDB:4OEE}.
SEQUENCE 288 AA; 30770 MW; EAE98552A39D5E19 CRC64;
MVGVGGGDVE DVTPRPGGCQ ISGRGARGCN GIPGAAAWEA ALPRRRPRRH PSVNPRSRAA
GSPRTRGRRT EERPSGSRLG DRGRGRALPG GRLGGRGRGR APERVGGRGR GRGTAAPRAA
PAARGSRPGP AGTMAAGSIT TLPALPEDGG SGAFPPGHFK DPKRLYCKNG GFFLRIHPDG
RVDGVREKSD PHIKLQLQAE ERGVVSIKGV CANRYLAMKE DGRLLASKCV TDECFFFERL
ESNNYNTYRS RKYTSWYVAL KRTGQYKLGS KTGPGQKAIL FLPMSAKS


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E0551c ELISA kit Basic fibroblast growth factor,bFGF,Chicken,FGF2,FGF-2,Gallus gallus,HBGF-2,Heparin-binding growth factor 2 96T
E0551c ELISA Basic fibroblast growth factor,bFGF,Chicken,FGF2,FGF-2,Gallus gallus,HBGF-2,Heparin-binding growth factor 2 96T
E0034m ELISA kit Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
E0034m ELISA Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
U0034m CLIA Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
10-271-82072 Fibroblast Growth Factor-basic Human - HBGF-2; Basic fibroblast growth factor; BFGF; Prostatropin 0.01 mg


 

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