GENTAUR Molecular Products.

 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.
 28-MAR-2018, entry version 216.
 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).
 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).
 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]
 INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, AND FUNCTION IN CELL
 PROLIFERATION.
 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]
 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).
 [34]
 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).
 [35]
 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).
 [36]
 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).
 [37]
 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).
 [38]
 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).
 [39]
 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: Plays an important role in the regulation of cell
     survival, cell division, angiogenesis, cell differentiation and
     cell migration. Functions as potent mitogen in vitro. Can induce
     angiogenesis (PubMed:23469107). {ECO:0000269|PubMed:1721615,
     ECO:0000269|PubMed:23469107, 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 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: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";
 -----------------------------------------------------------------------
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 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.
 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; -.
 ProteinModelPortal; P09038; -.
 SMR; P09038; -.
 BioGrid; 108538; 26.
 CORUM; P09038; -.
 DIP; DIP-4012N; -.
 IntAct; P09038; 15.
 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; -.
 DNASU; 2247; -.
 Ensembl; ENST00000608478; ENSP00000477134; ENSG00000138685. [P09038-2]
 Ensembl; ENST00000614010; ENSP00000478620; ENSG00000138685. [P09038-4]
 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: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:DFLAT.
 GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
 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: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}.
 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.
 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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