GenomeNet

Database: UniProt
Entry: P05230
LinkDB: P05230
Original site: P05230 
ID   FGF1_HUMAN              Reviewed;         155 AA.
AC   P05230; B2R5T0; D3DQF2; P07502; Q16588;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   31-JUL-2019, entry version 225.
DE   RecName: Full=Fibroblast growth factor 1;
DE            Short=FGF-1;
DE   AltName: Full=Acidic fibroblast growth factor;
DE            Short=aFGF;
DE   AltName: Full=Endothelial cell growth factor;
DE            Short=ECGF;
DE   AltName: Full=Heparin-binding growth factor 1;
DE            Short=HBGF-1;
DE   Flags: Precursor;
GN   Name=FGF1; Synonyms=FGFA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain stem;
RX   PubMed=3523756; DOI=10.1126/science.3523756;
RA   Jaye M., Howk R., Burgess W., Ricca G.A., Chiu I.-M., Ravera M.W.,
RA   O'Brien S.J., Modi W.S., Maciag T., Drohan W.N.;
RT   "Human endothelial cell growth factor: cloning, nucleotide sequence,
RT   and chromosome localization.";
RL   Science 233:541-545(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2590193; DOI=10.1016/0006-291X(89)91785-3;
RA   Mergia A., Tischer E., Graves D., Tumolo A., Miller J.,
RA   Gospodarowicz D., Abraham J.A., Shipley G.D., Fiddes J.C.;
RT   "Structural analysis of the gene for human acidic fibroblast growth
RT   factor.";
RL   Biochem. Biophys. Res. Commun. 164:1121-1129(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain stem;
RX   PubMed=2474753; DOI=10.1128/MCB.9.6.2387;
RA   Wang W.P., Lehtoma K., Varban M.L., Krishnan I., Chiu I.M.;
RT   "Cloning of the gene coding for human class 1 heparin-binding growth
RT   factor and its expression in fetal tissues.";
RL   Mol. Cell. Biol. 9:2387-2395(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain stem;
RX   PubMed=1693186;
RA   Chiu I.M., Wang W.P., Lehtoma K.;
RT   "Alternative splicing generates two forms of mRNA coding for human
RT   heparin-binding growth factor 1.";
RL   Oncogene 5:755-762(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1717925;
RA   Wang W.P., Quick D., Balcerzak S.P., Needleman S.W., Chiu I.M.;
RT   "Cloning and sequence analysis of the human acidic fibroblast growth
RT   factor gene and its preservation in leukemia patients.";
RL   Oncogene 6:1521-1529(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1372643; DOI=10.1084/jem.175.4.1073;
RA   Li Y.L., Kha H., Golden J.A., Migchielsen A.A.J., Goetzl E.J.,
RA   Turck E.J.;
RT   "An acidic fibroblast growth factor protein generated by alternate
RT   splicing acts like an antagonist.";
RL   J. Exp. Med. 175:1073-1080(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   1-154 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=7504343;
RA   Zhao X.M., Yeoh T.K., Hiebert M., Frist W.H., Miller G.G.;
RT   "The expression of acidic fibroblast growth factor (heparin-binding
RT   growth factor-1) and cytokine genes in human cardiac allografts and T
RT   cells.";
RL   Transplantation 56:1177-1182(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-21.
RG   NIEHS SNPs program;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA   Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA   Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA   Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA   Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA   Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA   Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA   Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA   Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-40 (ISOFORMS 1/2).
RX   PubMed=2393407; DOI=10.1016/0006-291X(90)91348-V;
RA   Crumley G., Dionne C.A., Jaye M.;
RT   "The gene for human acidic fibroblast growth factor encodes two
RT   upstream exons alternatively spliced to the first coding exon.";
RL   Biochem. Biophys. Res. Commun. 171:7-13(1990).
RN   [14]
RP   PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
RX   PubMed=2427112; DOI=10.1021/bi00362a017;
RA   Harper J.W., Strydom D.J., Lobb R.R.;
RT   "Human class 1 heparin-binding growth factor: structure and homology
RT   to bovine acidic brain fibroblast growth factor.";
RL   Biochemistry 25:4097-4103(1986).
RN   [15]
RP   PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
RX   PubMed=3527167; DOI=10.1016/S0006-291X(86)80540-X;
RA   Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.;
RT   "The complete amino acid sequence of human brain-derived acidic
RT   fibroblast growth factor.";
RL   Biochem. Biophys. Res. Commun. 138:611-617(1986).
RN   [16]
RP   PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
RX   PubMed=3778488; DOI=10.1016/0006-291X(86)90716-3;
RA   Gautschi-Sova P., Mueller T., Boehlen P.;
RT   "Amino acid sequence of human acidic fibroblast growth factor.";
RL   Biochem. Biophys. Res. Commun. 140:874-880(1986).
RN   [17]
RP   PROTEIN SEQUENCE OF 16-47 (ISOFORMS 1/2).
RX   PubMed=3964259; DOI=10.1016/0006-291X(86)90028-8;
RA   Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.;
RT   "Human brain-derived acidic and basic fibroblast growth factors: amino
RT   terminal sequences and specific mitogenic activities.";
RL   Biochem. Biophys. Res. Commun. 135:541-548(1986).
RN   [18]
RP   PROTEIN SEQUENCE OF 16-49 (ISOFORMS 1/2).
RX   PubMed=3732516; DOI=10.1016/0014-5793(86)80812-2;
RA   Gautschi P., Frater-Schroeder M., Boehlen P.;
RT   "Partial molecular characterization of endothelial cell mitogens from
RT   human brain: acidic and basic fibroblast growth factors.";
RL   FEBS Lett. 204:203-207(1986).
RN   [19]
RP   IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF2, AND INTERACTION WITH
RP   FGFBP1.
RX   PubMed=1885605;
RA   Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.;
RT   "Characterization and molecular cloning of a putative binding protein
RT   for heparin-binding growth factors.";
RL   J. Biol. Chem. 266:16778-16785(1991).
RN   [20]
RP   INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, AND FUNCTION IN CELL
RP   PROLIFERATION.
RX   PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
RA   Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
RA   Coulier F., Gao G., Goldfarb M.;
RT   "Receptor specificity of the fibroblast growth factor family.";
RL   J. Biol. Chem. 271:15292-15297(1996).
RN   [21]
RP   SUBCELLULAR LOCATION, COPPER-BINDING, AND INTERACTION WITH S100A13 AND
RP   SYT1.
RX   PubMed=11432880; DOI=10.1074/jbc.M102925200;
RA   Landriscina M., Bagala C., Mandinova A., Soldi R., Micucci I.,
RA   Bellum S., Prudovsky I., Maciag T.;
RT   "Copper induces the assembly of a multiprotein aggregate implicated in
RT   the release of fibroblast growth factor 1 in response to stress.";
RL   J. Biol. Chem. 276:25549-25557(2001).
RN   [22]
RP   INTERACTION WITH CSNK2A; CSNK2B; FGF2; FIBP AND LRRC59, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-114; SER-131 AND
RP   LYS-133.
RX   PubMed=11964394; DOI=10.1074/jbc.M112193200;
RA   Skjerpen C.S., Wesche J., Olsnes S.;
RT   "Identification of ribosome-binding protein p34 as an intracellular
RT   protein that binds acidic fibroblast growth factor.";
RL   J. Biol. Chem. 277:23864-23871(2002).
RN   [23]
RP   INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, AND FUNCTION IN
RP   STIMULATION OF CELL PROLIFERATION.
RX   PubMed=16597617; DOI=10.1074/jbc.M601252200;
RA   Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M.,
RA   Ornitz D.M.;
RT   "Receptor specificity of the fibroblast growth factor family. The
RT   complete mammalian FGF family.";
RL   J. Biol. Chem. 281:15694-15700(2006).
RN   [24]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18400376; DOI=10.1016/j.canlet.2008.03.001;
RA   Di Serio C., Doria L., Pellerito S., Prudovsky I., Micucci I.,
RA   Massi D., Landriscina M., Marchionni N., Masotti G., Tarantini F.;
RT   "The release of fibroblast growth factor-1 from melanoma cells
RT   requires copper ions and is mediated by phosphatidylinositol 3-
RT   kinase/Akt intracellular signaling pathway.";
RL   Cancer Lett. 267:67-74(2008).
RN   [25]
RP   FUNCTION, BINDING TO INTEGRIN; HEPARIN AND FGFR1, AND MUTAGENESIS OF
RP   ASN-33; ARG-50; GLU-102; TYR-109; ASN-110; LYS-127; LYS-128; LYS-133
RP   AND ARG-134.
RX   PubMed=18441324; DOI=10.1074/jbc.M801213200;
RA   Mori S., Wu C.Y., Yamaji S., Saegusa J., Shi B., Ma Z., Kuwabara Y.,
RA   Lam K.S., Isseroff R.R., Takada Y.K., Takada Y.;
RT   "Direct binding of integrin alphavbeta3 to FGF1 plays a role in FGF1
RT   signaling.";
RL   J. Biol. Chem. 283:18066-18075(2008).
RN   [26]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20863990; DOI=10.1016/S0929-6646(10)60103-9;
RA   Cao R., Yan B., Yang H., Zu X., Wen G., Zhong J.;
RT   "Effect of human S100A13 gene silencing on FGF-1 transportation in
RT   human endothelial cells.";
RL   J. Formos. Med. Assoc. 109:632-640(2010).
RN   [27]
RP   REVIEW.
RX   PubMed=15863030; DOI=10.1016/j.cytogfr.2005.01.001;
RA   Eswarakumar V.P., Lax I., Schlessinger J.;
RT   "Cellular signaling by fibroblast growth factor receptors.";
RL   Cytokine Growth Factor Rev. 16:139-149(2005).
RN   [28]
RP   REVIEW.
RX   PubMed=20094046; DOI=10.1038/nrc2780;
RA   Turner N., Grose R.;
RT   "Fibroblast growth factor signalling: from development to cancer.";
RL   Nat. Rev. Cancer 10:116-129(2010).
RN   [29]
RP   FUNCTION, BINDING TO FGFR1, IDENTIFICATION IN A COMPLEX WITH INTEGRIN
RP   AND FGFR1, AND MUTAGENESIS OF ARG-50.
RX   PubMed=20422052; DOI=10.1371/journal.pone.0010273;
RA   Yamaji S., Saegusa J., Ieguchi K., Fujita M., Mori S., Takada Y.K.,
RA   Takada Y.;
RT   "A novel fibroblast growth factor-1 (FGF1) mutant that acts as an FGF
RT   antagonist.";
RL   PLoS ONE 5:E10273-E10273(2010).
RN   [30]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP   24-LYS--LYS-27.
RX   PubMed=22321063; DOI=10.1111/j.1600-0854.2012.01341.x;
RA   Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y.,
RA   Walchli S., Olsnes S., Wiedlocha A.;
RT   "Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and
RT   the importins Kpnalpha1 and Kpnbeta1.";
RL   Traffic 13:650-664(2012).
RN   [31]
RP   FUNCTION, AND MUTAGENESIS OF ARG-50.
RX   PubMed=23469107; DOI=10.1371/journal.pone.0057927;
RA   Mori S., Tran V., Nishikawa K., Kaneda T., Hamada Y., Kawaguchi N.,
RA   Fujita M., Saegusa J., Takada Y.K., Matsuura N., Zhao M., Takada Y.;
RT   "A dominant-negative FGF1 mutant (the R50E mutant) suppresses
RT   tumorigenesis and angiogenesis.";
RL   PLoS ONE 8:E57927-E57927(2013).
RN   [32]
RP   ERRATUM.
RA   Mori S., Tran V., Nishikawa K., Kaneda T., Hamada Y., Kawaguchi N.,
RA   Fujita M., Saegusa J., Takada Y.K., Matsuura N., Zhao M., Takada Y.;
RL   PLoS ONE 8:E91599-E91599(2013).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-155.
RX   PubMed=1702556; DOI=10.1126/science.1702556;
RA   Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T.,
RA   Hsu B.T., Rees D.C.;
RT   "Three-dimensional structures of acidic and basic fibroblast growth
RT   factors.";
RL   Science 251:90-93(1991).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-155.
RX   PubMed=8652550; DOI=10.1021/bi9521755;
RA   Blaber M., Disalvo J., Thomas K.A.;
RT   "X-ray crystal structure of human acidic fibroblast growth factor.";
RL   Biochemistry 35:2086-2094(1996).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-155 IN COMPLEX WITH
RP   HEPARIN, AND SUBUNIT.
RX   PubMed=9655399; DOI=10.1038/31741;
RA   DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M.,
RA   Schlessinger J., Hendrickson W.A.;
RT   "Structure of a heparin-linked biologically active dimer of fibroblast
RT   growth factor.";
RL   Nature 393:812-817(1998).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-155 IN COMPLEX WITH FGFR1.
RX   PubMed=10830168; DOI=10.1016/S0092-8674(00)80851-X;
RA   Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.;
RT   "Crystal structures of two FGF-FGFR complexes reveal the determinants
RT   of ligand-receptor specificity.";
RL   Cell 101:413-424(2000).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-155 IN COMPLEX WITH FGFR2
RP   AND HEPARIN.
RX   PubMed=11069186; DOI=10.1038/35039551;
RA   Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.;
RT   "Crystal structure of fibroblast growth factor receptor ectodomain
RT   bound to ligand and heparin.";
RL   Nature 407:1029-1034(2000).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-155 IN COMPLEX WITH FGFR2.
RX   PubMed=10618369; DOI=10.1073/pnas.97.1.49;
RA   Stauber D.J., DiGabriele A.D., Hendrickson W.A.;
RT   "Structural interactions of fibroblast growth factor receptor with its
RT   ligands.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-155.
RX   PubMed=11847269; DOI=10.1110/ps.43802;
RA   Kim J., Blaber S.I., Blaber M.;
RT   "Alternative type I and I' turn conformations in the beta8/beta9 beta-
RT   hairpin of human acidic fibroblast growth factor.";
RL   Protein Sci. 11:459-466(2002).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FGFR3.
RX   PubMed=14732692; DOI=10.1073/pnas.0307287101;
RA   Olsen S.K., Ibrahimi O.A., Raucci A., Zhang F., Eliseenkova A.V.,
RA   Yayon A., Basilico C., Linhardt R.J., Schlessinger J., Mohammadi M.;
RT   "Insights into the molecular basis for fibroblast growth factor
RT   receptor autoinhibition and ligand-binding promiscuity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:935-940(2004).
RN   [41]
RP   STRUCTURE BY NMR OF 24-155 IN COMPLEX WITH INOSITOL HEXASULFATE, AND
RP   PROTEIN SEQUENCE OF 24-27.
RX   PubMed=7521397; DOI=10.1006/jmbi.1994.1558;
RA   Pineda-Lucena A., Jimenez M.A., Nieto J.L., Santoro J., Rico M.,
RA   Gimenez-Gallego G.;
RT   "1H-NMR assignment and solution structure of human acidic fibroblast
RT   growth factor activated by inositol hexasulfate.";
RL   J. Mol. Biol. 242:81-98(1994).
RN   [42]
RP   STRUCTURE BY NMR OF 24-155.
RX   PubMed=8950275; DOI=10.1006/jmbi.1996.0631;
RA   Pineda-Lucena A., Jimenez M.A., Lozano R.M., Nieto J.L., Santoro J.,
RA   Rico M., Gimenez-Gallego G.;
RT   "Three-dimensional structure of acidic fibroblast growth factor in
RT   solution: effects of binding to a heparin functional analog.";
RL   J. Mol. Biol. 264:162-178(1996).
RN   [43]
RP   STRUCTURE BY NMR OF 24-155.
RX   PubMed=9719643; DOI=10.1006/jmbi.1998.1977;
RA   Lozano R.M., Jimenez M., Santoro J., Rico M., Gimenez-Gallego G.;
RT   "Solution structure of acidic fibroblast growth factor bound to 1,3,
RT   6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action
RT   of suramins and suradistas.";
RL   J. Mol. Biol. 281:899-915(1998).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 24-153 IN COMPLEX WITH
RP   GENTISIC ACID AND 2,5-DIHYDROXYPHENYLSULFONATE, FUNCTION,
RP   HEPARIN-BINDING, AND INTERACTION WITH FGFR1.
RX   PubMed=20145243; DOI=10.1074/jbc.M109.064618;
RA   Fernandez I.S., Cuevas P., Angulo J., Lopez-Navajas P.,
RA   Canales-Mayordomo A., Gonzalez-Corrochano R., Lozano R.M.,
RA   Valverde S., Jimenez-Barbero J., Romero A., Gimenez-Gallego G.;
RT   "Gentisic acid, a compound associated with plant defense and a
RT   metabolite of aspirin, heads a new class of in vivo fibroblast growth
RT   factor inhibitors.";
RL   J. Biol. Chem. 285:11714-11729(2010).
RN   [45]
RP   STRUCTURE BY NMR OF 23-155.
RX   PubMed=20220137; DOI=10.1074/jbc.M109.066357;
RA   Mohan S.K., Rani S.G., Yu C.;
RT   "The heterohexameric complex structure, a component in the non-
RT   classical pathway for fibroblast growth factor 1 (FGF1) secretion.";
RL   J. Biol. Chem. 285:15464-15475(2010).
CC   -!- FUNCTION: Plays an important role in the regulation of cell
CC       survival, cell division, angiogenesis, cell differentiation and
CC       cell migration. Functions as potent mitogen in vitro. Acts as a
CC       ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of
CC       heparin leading to FGFR1 dimerization and activation via
CC       sequential autophosphorylation on tyrosine residues which act as
CC       docking sites for interacting proteins, leading to the activation
CC       of several signaling cascades. Binds to integrin ITGAV:ITGB3. Its
CC       binding to integrin, subsequent ternary complex formation with
CC       integrin and FGFR1, and the recruitment of PTPN11 to the complex
CC       are essential for FGF1 signaling. Induces the phosphorylation and
CC       activation of FGFR1, FRS2, MAPK3/ERK1, MAPK1/ERK2 and AKT1
CC       (PubMed:18441324, PubMed:20422052). Can induce angiogenesis
CC       (PubMed:23469107). {ECO:0000269|PubMed:16597617,
CC       ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:20145243,
CC       ECO:0000269|PubMed:20422052, ECO:0000269|PubMed:23469107,
CC       ECO:0000269|PubMed:8663044}.
CC   -!- SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3
CC       and FGFR4. Affinity between fibroblast growth factors (FGFs) and
CC       their receptors is increased by heparan sulfate glycosaminoglycans
CC       that function as coreceptors. Found in a complex with FGFBP1, FGF1
CC       and FGF2. Interacts with FGFBP1. Part of a Cu(2+)-dependent
CC       multiprotein aggregate containing FGF1, S100A13 and SYT1.
CC       Interacts with SYT1. Interacts with S100A13. Interacts with
CC       LRRC59. Interacts with CSNKA, CSNKB and FIBP. While binding with
CC       LRRC59, CSNKA and FIBP seem mutually exclusive, CSNKB and FIBP may
CC       cooperatively interact with FGF1. Forms a ternary complex with
CC       FGFR1 and ITGAV:ITGB3 and induces the recruitment of PTPN11 to the
CC       complex (PubMed:20422052). {ECO:0000269|PubMed:10618369,
CC       ECO:0000269|PubMed:10830168, ECO:0000269|PubMed:11069186,
CC       ECO:0000269|PubMed:11432880, ECO:0000269|PubMed:11964394,
CC       ECO:0000269|PubMed:14732692, ECO:0000269|PubMed:16597617,
CC       ECO:0000269|PubMed:1885605, ECO:0000269|PubMed:20145243,
CC       ECO:0000269|PubMed:20422052, ECO:0000269|PubMed:7521397,
CC       ECO:0000269|PubMed:8663044, ECO:0000269|PubMed:9655399}.
CC   -!- INTERACTION:
CC       P11362:FGFR1; NbExp=3; IntAct=EBI-698068, EBI-1028277;
CC       P21802:FGFR2; NbExp=2; IntAct=EBI-698068, EBI-1028658;
CC       P21802-1:FGFR2; NbExp=2; IntAct=EBI-15489950, EBI-15489960;
CC       P22607:FGFR3; NbExp=3; IntAct=EBI-698068, EBI-348399;
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex.
CC       Cytoplasm, cytosol. Nucleus. Note=Lacks a cleavable signal
CC       sequence. Within the cytoplasm, it is transported to the cell
CC       membrane and then secreted by a non-classical pathway that
CC       requires Cu(2+) ions and S100A13. Secreted in a complex with SYT1
CC       (By similarity). Binding of exogenous FGF1 to FGFR facilitates
CC       endocytosis followed by translocation of FGF1 across endosomal
CC       membrane into the cytosol. Nuclear import from the cytosol
CC       requires the classical nuclear import machinery, involving
CC       proteins KPNA1 and KPNB1, as well as LRRC59. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P05230-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P05230-2; Sequence=VSP_036536, VSP_036537;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and brain.
CC       Detected at much lower levels in heart and skeletal muscle.
CC       {ECO:0000269|PubMed:11964394, ECO:0000269|PubMed:7504343}.
CC   -!- PTM: In the nucleus, phosphorylated by PKC/PRKCD.
CC       {ECO:0000269|PubMed:22321063}.
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/fgf1/";
DR   EMBL; M13361; AAA79245.1; -; mRNA.
DR   EMBL; M30492; AAA52446.1; -; Genomic_DNA.
DR   EMBL; M30490; AAA52446.1; JOINED; Genomic_DNA.
DR   EMBL; M30491; AAA52446.1; JOINED; Genomic_DNA.
DR   EMBL; M23087; AAA52638.1; -; Genomic_DNA.
DR   EMBL; M23086; AAA52638.1; JOINED; Genomic_DNA.
DR   EMBL; X51943; CAA36206.1; -; mRNA.
DR   EMBL; X65778; CAA46661.1; -; mRNA.
DR   EMBL; S67291; AAB29057.2; -; mRNA.
DR   EMBL; S67292; AAB29058.1; -; mRNA.
DR   EMBL; AY601819; AAS99352.1; -; Genomic_DNA.
DR   EMBL; AC005370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK312301; BAG35227.1; -; mRNA.
DR   EMBL; CH471062; EAW61881.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61882.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW61885.1; -; Genomic_DNA.
DR   EMBL; BC032697; AAH32697.1; -; mRNA.
DR   EMBL; M60515; AAA51672.1; -; mRNA.
DR   EMBL; M60516; AAA51673.1; -; mRNA.
DR   CCDS; CCDS4275.1; -. [P05230-1]
DR   CCDS; CCDS4276.1; -. [P05230-2]
DR   PIR; A33665; A33665.
DR   PIR; JH0708; JH0708.
DR   RefSeq; NP_000791.1; NM_000800.4. [P05230-1]
DR   RefSeq; NP_001138364.1; NM_001144892.2. [P05230-1]
DR   RefSeq; NP_001138406.1; NM_001144934.1. [P05230-1]
DR   RefSeq; NP_001138407.1; NM_001144935.1. [P05230-1]
DR   RefSeq; NP_001244134.1; NM_001257205.1. [P05230-1]
DR   RefSeq; NP_001244136.1; NM_001257207.1. [P05230-1]
DR   RefSeq; NP_001244137.1; NM_001257208.1. [P05230-1]
DR   RefSeq; NP_001244138.1; NM_001257209.1. [P05230-1]
DR   RefSeq; NP_001244139.1; NM_001257210.1. [P05230-1]
DR   RefSeq; NP_149127.1; NM_033136.3. [P05230-2]
DR   PDB; 1AXM; X-ray; 3.00 A; A/B/C/D/E/F=21-155.
DR   PDB; 1DJS; X-ray; 2.40 A; B=21-155.
DR   PDB; 1DZC; NMR; -; A=25-155.
DR   PDB; 1DZD; NMR; -; A=29-155.
DR   PDB; 1E0O; X-ray; 2.80 A; A/C=16-155.
DR   PDB; 1EVT; X-ray; 2.80 A; A/B=22-155.
DR   PDB; 1HKN; X-ray; 2.00 A; A/B/C/D/E/F=17-155.
DR   PDB; 1JQZ; X-ray; 1.65 A; A/B=16-155.
DR   PDB; 1JT3; X-ray; 1.95 A; A/B=16-155.
DR   PDB; 1JT4; X-ray; 1.78 A; A/B=16-155.
DR   PDB; 1JT5; X-ray; 1.85 A; A/B=16-155.
DR   PDB; 1JT7; X-ray; 1.70 A; A/B/C/D=16-155.
DR   PDB; 1JTC; X-ray; 1.70 A; A/B/C/D=16-155.
DR   PDB; 1JY0; X-ray; 1.70 A; A/B=16-155.
DR   PDB; 1K5U; X-ray; 2.00 A; A/B/C=16-154.
DR   PDB; 1K5V; X-ray; 2.10 A; A/B=16-154.
DR   PDB; 1M16; X-ray; 1.70 A; A/B=16-155.
DR   PDB; 1NZK; X-ray; 1.95 A; A/B/C/D=16-152.
DR   PDB; 1P63; X-ray; 1.60 A; A/B=16-155.
DR   PDB; 1PZZ; X-ray; 2.00 A; A/B=16-155.
DR   PDB; 1Q03; X-ray; 2.05 A; A/B=16-152.
DR   PDB; 1Q04; X-ray; 1.80 A; A/B=16-155.
DR   PDB; 1QCT; Model; -; A/D=24-153.
DR   PDB; 1RG8; X-ray; 1.10 A; A/B=16-155.
DR   PDB; 1RML; NMR; -; A=1-155.
DR   PDB; 1RY7; X-ray; 3.20 A; A=1-155.
DR   PDB; 1YTO; X-ray; 2.10 A; A/B/C/D=16-155.
DR   PDB; 1Z2V; X-ray; 1.90 A; A/B=16-155.
DR   PDB; 1Z4S; X-ray; 2.60 A; A/B/C/D=16-155.
DR   PDB; 2AFG; X-ray; 2.00 A; A/B/C/D=16-155.
DR   PDB; 2AQZ; X-ray; 1.85 A; A/B=16-155.
DR   PDB; 2AXM; X-ray; 3.00 A; A/B=21-155.
DR   PDB; 2ERM; NMR; -; A=17-155.
DR   PDB; 2HW9; X-ray; 1.60 A; A/B=16-155.
DR   PDB; 2HWA; X-ray; 1.65 A; A/B=16-155.
DR   PDB; 2HWM; X-ray; 1.60 A; A/B=16-155.
DR   PDB; 2HZ9; X-ray; 1.70 A; A/B=16-155.
DR   PDB; 2K43; NMR; -; A=23-155.
DR   PDB; 2K4A; NMR; -; B=23-155.
DR   PDB; 2K8R; NMR; -; A=23-155.
DR   PDB; 2KI4; NMR; -; A/D=23-155.
DR   PDB; 2KI6; NMR; -; B/E=23-155.
DR   PDB; 2NTD; X-ray; 2.52 A; A/B/C/D=16-155.
DR   PDB; 2Q9X; X-ray; 1.70 A; A=16-155.
DR   PDB; 2RQ9; NMR; -; A=22-155.
DR   PDB; 3B9U; X-ray; 1.55 A; A=16-155.
DR   PDB; 3BA4; X-ray; 1.80 A; A/B=16-155.
DR   PDB; 3BA5; X-ray; 1.75 A; A/B=16-155.
DR   PDB; 3BA7; X-ray; 1.60 A; A/B=16-155.
DR   PDB; 3BAD; X-ray; 2.00 A; A/B=16-155.
DR   PDB; 3BAG; X-ray; 1.75 A; A/B=16-155.
DR   PDB; 3BAH; X-ray; 1.65 A; A/B=16-155.
DR   PDB; 3BAO; X-ray; 1.55 A; A/B=16-155.
DR   PDB; 3BAQ; X-ray; 1.80 A; A/B=16-155.
DR   PDB; 3BAU; X-ray; 1.60 A; A/B=16-155.
DR   PDB; 3BAV; X-ray; 1.62 A; A/B=16-155.
DR   PDB; 3BB2; X-ray; 1.50 A; A/B=16-155.
DR   PDB; 3CQA; X-ray; 1.80 A; A/B=16-155.
DR   PDB; 3CRG; X-ray; 1.85 A; A/B=16-155.
DR   PDB; 3CRH; X-ray; 2.15 A; A/B=16-155.
DR   PDB; 3CRI; X-ray; 2.10 A; A/B=16-155.
DR   PDB; 3CU1; X-ray; 2.60 A; B/D=22-152.
DR   PDB; 3FGM; X-ray; 1.95 A; A/B=16-155.
DR   PDB; 3FJ8; X-ray; 2.00 A; A/B=16-155.
DR   PDB; 3FJ9; X-ray; 1.90 A; A/B=16-155.
DR   PDB; 3FJA; X-ray; 1.95 A; A/B=16-155.
DR   PDB; 3FJB; X-ray; 2.00 A; A/B=16-155.
DR   PDB; 3FJC; X-ray; 2.00 A; A/B=16-155.
DR   PDB; 3FJD; X-ray; 1.90 A; A/B=16-155.
DR   PDB; 3FJE; X-ray; 2.10 A; A/B=16-155.
DR   PDB; 3FJF; X-ray; 1.90 A; A/B=16-155.
DR   PDB; 3FJH; X-ray; 1.90 A; A/B=16-155.
DR   PDB; 3FJI; X-ray; 2.55 A; A/B/C/D=16-155.
DR   PDB; 3FJJ; X-ray; 1.90 A; A/B=16-155.
DR   PDB; 3FJK; X-ray; 2.15 A; A/B/C/D=16-155.
DR   PDB; 3HOM; X-ray; 2.30 A; A/B=16-155.
DR   PDB; 3JUT; X-ray; 2.25 A; A/B/C/D/E/F=24-153.
DR   PDB; 3K1X; X-ray; 1.98 A; A/B/C/D/E/F=24-153.
DR   PDB; 3O3Q; X-ray; 1.60 A; A/B/C/D=16-155.
DR   PDB; 3OJ2; X-ray; 2.20 A; A/B=1-155.
DR   PDB; 3OJM; X-ray; 2.10 A; A=1-155.
DR   PDB; 3OJV; X-ray; 2.60 A; A/B=21-155.
DR   PDB; 3UD7; X-ray; 2.80 A; A/B/C=16-155.
DR   PDB; 3UD8; X-ray; 2.37 A; A/B/C=16-155.
DR   PDB; 3UD9; X-ray; 2.34 A; A/B/C=16-155.
DR   PDB; 3UDA; X-ray; 2.51 A; A/B/C=16-155.
DR   PDB; 4J23; X-ray; 3.88 A; B=21-155.
DR   PDB; 4Q91; X-ray; 1.80 A; A/B=16-155.
DR   PDB; 4Q9G; X-ray; 1.55 A; A/B=16-155.
DR   PDB; 4Q9P; X-ray; 1.80 A; A/B=16-155.
DR   PDB; 4QAL; X-ray; 1.50 A; A/B=16-155.
DR   PDB; 4QBC; X-ray; 1.52 A; A/B=16-155.
DR   PDB; 4QBV; X-ray; 1.50 A; A/B=16-155.
DR   PDB; 4QC4; X-ray; 1.49 A; A/B=16-155.
DR   PDB; 4QO3; X-ray; 2.05 A; A/B=16-155.
DR   PDB; 4XKI; X-ray; 2.00 A; A/B=16-155.
DR   PDB; 4YOL; X-ray; 1.97 A; A/B=16-155.
DR   PDBsum; 1AXM; -.
DR   PDBsum; 1DJS; -.
DR   PDBsum; 1DZC; -.
DR   PDBsum; 1DZD; -.
DR   PDBsum; 1E0O; -.
DR   PDBsum; 1EVT; -.
DR   PDBsum; 1HKN; -.
DR   PDBsum; 1JQZ; -.
DR   PDBsum; 1JT3; -.
DR   PDBsum; 1JT4; -.
DR   PDBsum; 1JT5; -.
DR   PDBsum; 1JT7; -.
DR   PDBsum; 1JTC; -.
DR   PDBsum; 1JY0; -.
DR   PDBsum; 1K5U; -.
DR   PDBsum; 1K5V; -.
DR   PDBsum; 1M16; -.
DR   PDBsum; 1NZK; -.
DR   PDBsum; 1P63; -.
DR   PDBsum; 1PZZ; -.
DR   PDBsum; 1Q03; -.
DR   PDBsum; 1Q04; -.
DR   PDBsum; 1QCT; -.
DR   PDBsum; 1RG8; -.
DR   PDBsum; 1RML; -.
DR   PDBsum; 1RY7; -.
DR   PDBsum; 1YTO; -.
DR   PDBsum; 1Z2V; -.
DR   PDBsum; 1Z4S; -.
DR   PDBsum; 2AFG; -.
DR   PDBsum; 2AQZ; -.
DR   PDBsum; 2AXM; -.
DR   PDBsum; 2ERM; -.
DR   PDBsum; 2HW9; -.
DR   PDBsum; 2HWA; -.
DR   PDBsum; 2HWM; -.
DR   PDBsum; 2HZ9; -.
DR   PDBsum; 2K43; -.
DR   PDBsum; 2K4A; -.
DR   PDBsum; 2K8R; -.
DR   PDBsum; 2KI4; -.
DR   PDBsum; 2KI6; -.
DR   PDBsum; 2NTD; -.
DR   PDBsum; 2Q9X; -.
DR   PDBsum; 2RQ9; -.
DR   PDBsum; 3B9U; -.
DR   PDBsum; 3BA4; -.
DR   PDBsum; 3BA5; -.
DR   PDBsum; 3BA7; -.
DR   PDBsum; 3BAD; -.
DR   PDBsum; 3BAG; -.
DR   PDBsum; 3BAH; -.
DR   PDBsum; 3BAO; -.
DR   PDBsum; 3BAQ; -.
DR   PDBsum; 3BAU; -.
DR   PDBsum; 3BAV; -.
DR   PDBsum; 3BB2; -.
DR   PDBsum; 3CQA; -.
DR   PDBsum; 3CRG; -.
DR   PDBsum; 3CRH; -.
DR   PDBsum; 3CRI; -.
DR   PDBsum; 3CU1; -.
DR   PDBsum; 3FGM; -.
DR   PDBsum; 3FJ8; -.
DR   PDBsum; 3FJ9; -.
DR   PDBsum; 3FJA; -.
DR   PDBsum; 3FJB; -.
DR   PDBsum; 3FJC; -.
DR   PDBsum; 3FJD; -.
DR   PDBsum; 3FJE; -.
DR   PDBsum; 3FJF; -.
DR   PDBsum; 3FJH; -.
DR   PDBsum; 3FJI; -.
DR   PDBsum; 3FJJ; -.
DR   PDBsum; 3FJK; -.
DR   PDBsum; 3HOM; -.
DR   PDBsum; 3JUT; -.
DR   PDBsum; 3K1X; -.
DR   PDBsum; 3O3Q; -.
DR   PDBsum; 3OJ2; -.
DR   PDBsum; 3OJM; -.
DR   PDBsum; 3OJV; -.
DR   PDBsum; 3UD7; -.
DR   PDBsum; 3UD8; -.
DR   PDBsum; 3UD9; -.
DR   PDBsum; 3UDA; -.
DR   PDBsum; 4J23; -.
DR   PDBsum; 4Q91; -.
DR   PDBsum; 4Q9G; -.
DR   PDBsum; 4Q9P; -.
DR   PDBsum; 4QAL; -.
DR   PDBsum; 4QBC; -.
DR   PDBsum; 4QBV; -.
DR   PDBsum; 4QC4; -.
DR   PDBsum; 4QO3; -.
DR   PDBsum; 4XKI; -.
DR   PDBsum; 4YOL; -.
DR   SMR; P05230; -.
DR   BioGrid; 108537; 28.
DR   CORUM; P05230; -.
DR   DIP; DIP-3787N; -.
DR   IntAct; P05230; 8.
DR   MINT; P05230; -.
DR   STRING; 9606.ENSP00000480791; -.
DR   BindingDB; P05230; -.
DR   ChEMBL; CHEMBL2120; -.
DR   DrugBank; DB08238; 5-AMINO-NAPHTALENE-2-MONOSULFONATE.
DR   DrugBank; DB01025; Amlexanox.
DR   DrugBank; DB01942; Formic Acid.
DR   DrugBank; DB04409; Naphthalene Trisulfonate.
DR   DrugBank; DB02264; O2-Sulfo-Glucuronic Acid.
DR   DrugBank; DB06589; Pazopanib.
DR   DrugBank; DB00686; Pentosan Polysulfate.
DR   DrugBank; DB01901; Sucrosofate.
DR   iPTMnet; P05230; -.
DR   PhosphoSitePlus; P05230; -.
DR   BioMuta; FGF1; -.
DR   DMDM; 122737; -.
DR   EPD; P05230; -.
DR   MaxQB; P05230; -.
DR   PaxDb; P05230; -.
DR   PeptideAtlas; P05230; -.
DR   PRIDE; P05230; -.
DR   ProteomicsDB; 51826; -. [P05230-1]
DR   ProteomicsDB; 51827; -. [P05230-2]
DR   TopDownProteomics; P05230-1; -. [P05230-1]
DR   ABCD; P05230; -.
DR   DNASU; 2246; -.
DR   Ensembl; ENST00000337706; ENSP00000338548; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000359370; ENSP00000352329; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000360966; ENSP00000354231; ENSG00000113578. [P05230-2]
DR   Ensembl; ENST00000378046; ENSP00000367285; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000419524; ENSP00000396195; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000441680; ENSP00000404742; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000610990; ENSP00000481868; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000612258; ENSP00000479024; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000619447; ENSP00000480980; ENSG00000113578. [P05230-1]
DR   Ensembl; ENST00000621536; ENSP00000480791; ENSG00000113578. [P05230-1]
DR   GeneID; 2246; -.
DR   KEGG; hsa:2246; -.
DR   UCSC; uc003lmm.5; human. [P05230-1]
DR   CTD; 2246; -.
DR   DisGeNET; 2246; -.
DR   GeneCards; FGF1; -.
DR   HGNC; HGNC:3665; FGF1.
DR   HPA; CAB017519; -.
DR   HPA; HPA003265; -.
DR   MIM; 131220; gene.
DR   neXtProt; NX_P05230; -.
DR   OpenTargets; ENSG00000113578; -.
DR   PharmGKB; PA28105; -.
DR   eggNOG; KOG3885; Eukaryota.
DR   eggNOG; ENOG4111IPH; LUCA.
DR   GeneTree; ENSGT00940000160557; -.
DR   HOGENOM; HOG000236341; -.
DR   InParanoid; P05230; -.
DR   KO; K18496; -.
DR   OMA; PRTHIGQ; -.
DR   OrthoDB; 1157770at2759; -.
DR   PhylomeDB; P05230; -.
DR   TreeFam; TF317805; -.
DR   Reactome; R-HSA-109704; PI3K Cascade.
DR   Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-HSA-1839122; Signaling by activated point mutants of FGFR1.
DR   Reactome; R-HSA-1839130; Signaling by activated point mutants of FGFR3.
DR   Reactome; R-HSA-190322; FGFR4 ligand binding and activation.
DR   Reactome; R-HSA-190370; FGFR1b ligand binding and activation.
DR   Reactome; R-HSA-190371; FGFR3b ligand binding and activation.
DR   Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
DR   Reactome; R-HSA-190373; FGFR1c ligand binding and activation.
DR   Reactome; R-HSA-190375; FGFR2c ligand binding and activation.
DR   Reactome; R-HSA-190377; FGFR2b ligand binding and activation.
DR   Reactome; R-HSA-2033514; FGFR3 mutant receptor activation.
DR   Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
DR   Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR   Reactome; R-HSA-5654219; Phospholipase C-mediated cascade: FGFR1.
DR   Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
DR   Reactome; R-HSA-5654227; Phospholipase C-mediated cascade, FGFR3.
DR   Reactome; R-HSA-5654228; Phospholipase C-mediated cascade, FGFR4.
DR   Reactome; R-HSA-5654687; Downstream signaling of activated FGFR1.
DR   Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
DR   Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
DR   Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
DR   Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
DR   Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
DR   Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
DR   Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
DR   Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
DR   Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
DR   Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
DR   Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
DR   Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
DR   Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
DR   Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
DR   Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
DR   Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
DR   Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
DR   Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR   Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
DR   SignaLink; P05230; -.
DR   SIGNOR; P05230; -.
DR   ChiTaRS; FGF1; human.
DR   EvolutionaryTrace; P05230; -.
DR   GeneWiki; FGF1; -.
DR   GenomeRNAi; 2246; -.
DR   PRO; PR:P05230; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000113578; Expressed in 171 organ(s), highest expression level in metanephric glomerulus.
DR   ExpressionAtlas; P05230; baseline and differential.
DR   Genevisible; P05230; HS.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005104; F:fibroblast growth factor receptor binding; IMP:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; IMP:UniProtKB.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IMP:UniProtKB.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0060681; P:branch elongation involved in ureteric bud branching; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0072163; P:mesonephric epithelium development; IDA:UniProtKB.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0001759; P:organ induction; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; IDA:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:1902533; P:positive regulation of intracellular signal transduction; IDA:BHF-UCL.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
DR   GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:2000544; P:regulation of endothelial cell chemotaxis to fibroblast growth factor; IDA:UniProtKB.
DR   GO; GO:1901509; P:regulation of endothelial tube morphogenesis; IMP:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR   CDD; cd00058; FGF; 1.
DR   InterPro; IPR028210; FGF1.
DR   InterPro; IPR002209; Fibroblast_GF_fam.
DR   InterPro; IPR008996; IL1/FGF.
DR   PANTHER; PTHR11486; PTHR11486; 1.
DR   PANTHER; PTHR11486:SF86; PTHR11486:SF86; 1.
DR   Pfam; PF00167; FGF; 1.
DR   PRINTS; PR00263; HBGFFGF.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF50353; SSF50353; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Angiogenesis;
KW   Complete proteome; Cytoplasm; Developmental protein; Differentiation;
KW   Direct protein sequencing; Growth factor; Heparin-binding; Mitogen;
KW   Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Secreted.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P03968}.
FT   PROPEP        2     15
FT                                /FTId=PRO_0000008907.
FT   CHAIN        16    155       Fibroblast growth factor 1.
FT                                /FTId=PRO_0000008908.
FT   REGION      127    143       Heparin-binding.
FT   MOTIF        24     27       Nuclear localization signal.
FT   BINDING      33     33       Heparin. {ECO:0000269|PubMed:11069186,
FT                                ECO:0000269|PubMed:9655399}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:P03968}.
FT   VAR_SEQ      57     60       IQLQ -> TDTK (in isoform 2).
FT                                {ECO:0000303|PubMed:7504343}.
FT                                /FTId=VSP_036536.
FT   VAR_SEQ      61    155       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7504343}.
FT                                /FTId=VSP_036537.
FT   VARIANT      21     21       G -> E (in dbSNP:rs17223632).
FT                                {ECO:0000269|Ref.8}.
FT                                /FTId=VAR_021357.
FT   MUTAGEN      24     27       KKPK->AAPA: Loss of nuclear import
FT                                leading to loss of phosphorylation by
FT                                PKC/PRKCD. {ECO:0000269|PubMed:22321063}.
FT   MUTAGEN      33     33       N->A: No effect on integrin-binding.
FT                                {ECO:0000269|PubMed:18441324}.
FT   MUTAGEN      50     50       R->E: Dominant-negative mutant. Defective
FT                                in integrin-binding and in ternary
FT                                complex formation with integrin and
FT                                FGFR1. No effect on heparin- and FGFR1-
FT                                binding. Defective in inducing FGF1
FT                                signaling, cell proliferation and cell
FT                                migration. Defective in inducing
FT                                angiogenesis, and suppression of
FT                                angiogenesis in different in vitro and in
FT                                vivo angiogenesis models.
FT                                {ECO:0000269|PubMed:18441324,
FT                                ECO:0000269|PubMed:20422052,
FT                                ECO:0000269|PubMed:23469107}.
FT   MUTAGEN     102    102       E->A: No effect on integrin-binding. No
FT                                effect on integrin- and heparin-binding,
FT                                loss of FGFR1-binding, defective in
FT                                inducing FGF1 signaling, cell
FT                                proliferation and cell migration; when
FT                                associated with A-109 and A-110.
FT                                {ECO:0000269|PubMed:18441324}.
FT   MUTAGEN     109    109       Y->A: No effect on integrin- and heparin-
FT                                binding, loss of FGFR1-binding, defective
FT                                in inducing FGF1 signaling, cell
FT                                proliferation and cell migration; when
FT                                associated with A-102 and A-110.
FT                                {ECO:0000269|PubMed:18441324}.
FT   MUTAGEN     110    110       N->A: No effect on integrin-binding. No
FT                                effect on integrin- and heparin-binding,
FT                                loss of FGFR1-binding, defective in
FT                                inducing FGF1 signaling, cell
FT                                proliferation and cell migration; when
FT                                associated with A-102 and A-109.
FT                                {ECO:0000269|PubMed:18441324}.
FT   MUTAGEN     114    114       S->A: Decrease in LRRC59-binding.
FT                                {ECO:0000269|PubMed:11964394}.
FT   MUTAGEN     127    127       K->E: Reduced integrin-binding; when
FT                                associated with E-128. Defective in
FT                                integrin-, heparin- and FGFR1-binding,
FT                                and defective in inducing FGF1 signaling,
FT                                cell proliferation and cell migration;
FT                                when associated with E-128; E-133 and E-
FT                                134. {ECO:0000269|PubMed:18441324}.
FT   MUTAGEN     128    128       K->E: Reduced integrin-binding; when
FT                                associated with E-127. Defective in
FT                                integrin-, heparin- and FGFR1-binding,
FT                                and defective in inducing FGF1 signaling,
FT                                cell proliferation and cell migration;
FT                                when associated with E-127; E-133 and E-
FT                                134. {ECO:0000269|PubMed:18441324}.
FT   MUTAGEN     131    131       S->A: Decrease in LRRC59-binding.
FT                                {ECO:0000269|PubMed:11964394}.
FT   MUTAGEN     131    131       S->E: Decrease in LRRC59-binding.
FT                                {ECO:0000269|PubMed:11964394}.
FT   MUTAGEN     133    133       K->A: Loss of LRRC59-binding.
FT                                {ECO:0000269|PubMed:11964394}.
FT   MUTAGEN     133    133       K->E: Loss of CSNK2A-, CSNK2B- and
FT                                LRRC59-binding. Reduced integrin-binding;
FT                                when associated with E-134. Defective in
FT                                integrin-, heparin- and FGFR1-binding,
FT                                and defective in inducing FGF1 signaling,
FT                                cell proliferation and cell migration;
FT                                when associated with E-128; E-133 and E-
FT                                134. {ECO:0000269|PubMed:11964394,
FT                                ECO:0000269|PubMed:18441324}.
FT   MUTAGEN     133    133       K->R: No effect on LRRC59-binding.
FT                                {ECO:0000269|PubMed:11964394}.
FT   MUTAGEN     134    134       R->E: Reduced integrin-binding; when
FT                                associated with E-133. Defective in
FT                                integrin-, heparin- and FGFR1-binding,
FT                                and defective in inducing FGF1 signaling,
FT                                cell proliferation and cell migration;
FT                                when associated with E-127; E-128 and E-
FT                                133. {ECO:0000269|PubMed:18441324}.
FT   TURN         11     13       {ECO:0000244|PDB:3OJM}.
FT   STRAND       23     25       {ECO:0000244|PDB:1RG8}.
FT   STRAND       27     31       {ECO:0000244|PDB:1RG8}.
FT   TURN         32     35       {ECO:0000244|PDB:1RG8}.
FT   STRAND       36     40       {ECO:0000244|PDB:1RG8}.
FT   TURN         42     44       {ECO:0000244|PDB:1DZC}.
FT   STRAND       46     49       {ECO:0000244|PDB:1RG8}.
FT   HELIX        55     57       {ECO:0000244|PDB:3B9U}.
FT   STRAND       59     65       {ECO:0000244|PDB:1RG8}.
FT   STRAND       68     73       {ECO:0000244|PDB:1RG8}.
FT   TURN         74     76       {ECO:0000244|PDB:1RG8}.
FT   STRAND       79     82       {ECO:0000244|PDB:1RG8}.
FT   STRAND       84     86       {ECO:0000244|PDB:3OJ2}.
FT   STRAND       88     93       {ECO:0000244|PDB:1RG8}.
FT   HELIX        96     98       {ECO:0000244|PDB:1RG8}.
FT   STRAND      100    105       {ECO:0000244|PDB:1RG8}.
FT   TURN        106    108       {ECO:0000244|PDB:1RG8}.
FT   STRAND      109    115       {ECO:0000244|PDB:1RG8}.
FT   HELIX       118    120       {ECO:0000244|PDB:1RG8}.
FT   STRAND      123    126       {ECO:0000244|PDB:3O3Q}.
FT   STRAND      130    132       {ECO:0000244|PDB:4QC4}.
FT   HELIX       135    137       {ECO:0000244|PDB:1RG8}.
FT   TURN        138    141       {ECO:0000244|PDB:2K43}.
FT   HELIX       143    145       {ECO:0000244|PDB:3B9U}.
FT   STRAND      147    151       {ECO:0000244|PDB:1RG8}.
SQ   SEQUENCE   155 AA;  17460 MW;  F586E8BFB09F1580 CRC64;
     MAEGEITTFT ALTEKFNLPP GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR DRSDQHIQLQ
     LSAESVGEVY IKSTETGQYL AMDTDGLLYG SQTPNEECLF LERLEENHYN TYISKKHAEK
     NWFVGLKKNG SCKRGPRTHY GQKAILFLPL PVSSD
//
DBGET integrated database retrieval system