FGF1

From Wikipedia, the free encyclopedia

Fibroblast growth factor 1 (acidic)

PDB rendering based on 1afc.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes

1AXM, 1DJS, 1DZC, 1DZD, 1E0O, 1EVT, 1HKN, 1JQZ, 1JT3, 1JT4, 1JT5, 1JT7, 1JTC, 1JY0, 1K5U, 1K5V, 1M16, 1NZK, 1P63, 1PZZ, 1Q03, 1Q04, 1RG8, 1RML, 1RY7, 1YTO, 1Z2V, 1Z4S, 2AFG, 2AQZ, 2AXM, 2ERM, 2HW9, 2HWA, 2HWM, 2HZ9, 2K43, 2K4A, 2K8R, 2KI4, 2KI6, 2NTD, 2Q9X, 2RQ9, 3B9U, 3BA4, 3BA5, 3BA7, 3BAD, 3BAG, 3BAH, 3BAO, 3BAQ, 3BAU, 3BAV, 3BB2, 3CQA, 3CRG, 3CRH, 3CRI, 3CU1, 3FGM, 3FJ8, 3FJ9, 3FJA, 3FJB, 3FJC, 3FJD, 3FJE, 3FJF, 3FJH, 3FJI, 3FJJ, 3FJK, 3HOM, 3JUT, 3K1X, 3O3Q, 3OJ2, 3OJM, 3OJV, 3UD7, 3UD8, 3UD9, 3UDA

Identifiers

Symbols

FGF1; AFGF; ECGF; ECGF-beta; ECGFA; ECGFB; FGF-1; FGF-alpha; FGFA; GLIO703; HBGF-1; HBGF1

External IDs

OMIM: 131220 MGI: 95515 HomoloGene: 625 ChEMBL: 2120 GeneCards: FGF1 Gene

Gene Ontology
Molecular function	• fibroblast growth factor receptor binding • protein binding • growth factor activity • heparin binding • Hsp70 protein binding • S100 protein binding
Cellular component	• extracellular region • proteinaceous extracellular matrix • extracellular space • nucleolus • cytosol • cell cortex
Biological process	• angiogenesis • organ induction • positive regulation of protein phosphorylation • signal transduction • epidermal growth factor receptor signaling pathway • multicellular organismal development • positive regulation of cell proliferation • insulin receptor signaling pathway • fibroblast growth factor receptor signaling pathway • anatomical structure morphogenesis • positive regulation of intracellular protein kinase cascade • lung development • positive regulation of cell migration • cellular response to heat • innate immune response • positive regulation of cholesterol biosynthetic process • positive regulation of angiogenesis • positive regulation of transcription from RNA polymerase II promoter • neurotrophin TRK receptor signaling pathway • phosphatidylinositol-mediated signaling • positive regulation of epithelial cell proliferation • positive regulation of cell division • branch elongation involved in ureteric bud branching • mesonephric epithelium development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
141.97 – 142.08 Mb

Chr 18:
38.84 – 38.93 Mb

PubMed search

Heparin-binding growth factor 1 is a protein that in humans is encoded by the FGF1 gene.^[1]^[2]

The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described.^[3]

Interactions

FGF1 has been shown to interact with CSNK2B,^[4] CSNK2A2,^[4] HSPA9,^[5] S100A13,^[6]^[7] Casein kinase 2, alpha 1,^[4] Fibroblast growth factor receptor 1,^[8]^[9] FIBP,^[10] Fibroblast growth factor receptor 4,^[11]^[12] Fibroblast growth factor receptor 2^[9]^[13]^[14] and Fibroblast growth factor receptor 3.^[9]^[15]

References

↑ Dionne CA, Crumley G, Bellot F, Kaplow JM, Searfoss G, Ruta M, Burgess WH, Jaye M, Schlessinger J (October 1990). "Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors". EMBO J 9 (9): 2685–92. PMC 551973. PMID 1697263.
↑ Jaye M, Howk R, Burgess W, Ricca GA, Chiu IM, Ravera MW, O'Brien SJ, Modi WS, Maciag T, Drohan WN (August 1986). "Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization". Science 233 (4763): 541–5. doi:10.1126/science.3523756. PMID 3523756.
↑ "Entrez Gene: FGF1 fibroblast growth factor 1 (acidic)".
↑ 4.0 4.1 4.2 Skjerpen, Camilla Skiple; Nilsen Trine, Wesche Jørgen, Olsnes Sjur (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". EMBO J. (England) 21 (15): 4058–69. doi:10.1093/emboj/cdf402. ISSN 0261-4189. PMC 126148. PMID 12145206. Cite uses deprecated parameters (help)
↑ Mizukoshi, E; Suzuki M, Loupatov A, Uruno T, Hayashi H, Misono T, Kaul S C, Wadhwa R, Imamura T (October 1999). "Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin". Biochem. J. (ENGLAND) 343 (2): 461–6. doi:10.1042/0264-6021:3430461. ISSN 0264-6021. PMC 1220575. PMID 10510314. Cite uses deprecated parameters (help)
↑ Mouta Carreira, C; LaVallee T M, Tarantini F, Jackson A, Lathrop J T, Hampton B, Burgess W H, Maciag T (August 1998). "S100A13 is involved in the regulation of fibroblast growth factor-1 and p40 synaptotagmin-1 release in vitro". J. Biol. Chem. (UNITED STATES) 273 (35): 22224–31. doi:10.1074/jbc.273.35.22224. ISSN 0021-9258. PMID 9712836. Cite uses deprecated parameters (help)
↑ Landriscina, M; Bagalá C, Mandinova A, Soldi R, Micucci I, Bellum S, Prudovsky I, Maciag T (July 2001). "Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress". J. Biol. Chem. (United States) 276 (27): 25549–57. doi:10.1074/jbc.M102925200. ISSN 0021-9258. PMID 11432880. Cite uses deprecated parameters (help)
↑ Schlessinger, J; Plotnikov A N, Ibrahimi O A, Eliseenkova A V, Yeh B K, Yayon A, Linhardt R J, Mohammadi M (September 2000). "Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization". Mol. Cell (UNITED STATES) 6 (3): 743–50. doi:10.1016/S1097-2765(00)00073-3. ISSN 1097-2765. PMID 11030354. Cite uses deprecated parameters (help)
↑ 9.0 9.1 9.2 Santos-Ocampo, S; Colvin J S, Chellaiah A, Ornitz D M (January 1996). "Expression and biological activity of mouse fibroblast growth factor-9". J. Biol. Chem. (UNITED STATES) 271 (3): 1726–31. doi:10.1074/jbc.271.3.1726. ISSN 0021-9258. PMID 8576175. Cite uses deprecated parameters (help)
↑ Kolpakova, E; Wiedłocha A, Stenmark H, Klingenberg O, Falnes P O, Olsnes S (November 1998). "Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor". Biochem. J. (ENGLAND) 336 (Pt 1): 213–22. ISSN 0264-6021. PMC 1219860. PMID 9806903. Cite uses deprecated parameters (help)
↑ Loo, B B; Darwish K K, Vainikka S S, Saarikettu J J, Vihko P P, Hermonen J J, Goldman A A, Alitalo K K, Jalkanen M M (May 2000). "Production and characterization of the extracellular domain of recombinant human fibroblast growth factor receptor 4". Int. J. Biochem. Cell Biol. (ENGLAND) 32 (5): 489–97. doi:10.1016/S1357-2725(99)00145-4. ISSN 1357-2725. PMID 10736564. Cite uses deprecated parameters (help)
↑ Kan, M; Wu X, Wang F, McKeehan W L (May 1999). "Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase". J. Biol. Chem. (UNITED STATES) 274 (22): 15947–52. doi:10.1074/jbc.274.22.15947. ISSN 0021-9258. PMID 10336501. Cite uses deprecated parameters (help)
↑ Stauber, D J; DiGabriele A D, Hendrickson W A (January 2000). "Structural interactions of fibroblast growth factor receptor with its ligands". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (1): 49–54. doi:10.1073/pnas.97.1.49. ISSN 0027-8424. PMC 26614. PMID 10618369. Cite uses deprecated parameters (help)
↑ Pellegrini, L; Burke D F, von Delft F, Mulloy B, Blundell T L (October 2000). "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin". Nature (ENGLAND) 407 (6807): 1029–34. doi:10.1038/35039551. ISSN 0028-0836. PMID 11069186. Cite uses deprecated parameters (help)
↑ Chellaiah, A; Yuan W, Chellaiah M, Ornitz D M (December 1999). "Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity". J. Biol. Chem. (UNITED STATES) 274 (49): 34785–94. doi:10.1074/jbc.274.49.34785. ISSN 0021-9258. PMID 10574949. Cite uses deprecated parameters (help)

Yu YL, Kha H, Golden JA, et al. (1992). "An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist". J. Exp. Med. 175 (4): 1073–80. doi:10.1084/jem.175.4.1073. PMC 2119192. PMID 1372643.
Chiu IM, Wang WP, Lehtoma K (1990). "Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1". Oncogene 5 (5): 755–62. PMID 1693186.
Zhu X, Komiya H, Chirino A, et al. (1991). "Three-dimensional structures of acidic and basic fibroblast growth factors". Science 251 (4989): 90–3. doi:10.1126/science.1702556. PMID 1702556.
Wang WP, Quick D, Balcerzak SP, et al. (1991). "Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients". Oncogene 6 (9): 1521–9. PMID 1717925.
Wu DQ, Kan MK, Sato GH, et al. (1991). "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors". J. Biol. Chem. 266 (25): 16778–85. PMID 1885605.
Crumley G, Dionne CA, Jaye M (1990). "The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon". Biochem. Biophys. Res. Commun. 171 (1): 7–13. doi:10.1016/0006-291X(90)91348-V. PMID 2393407.
Harper JW, Strydom DJ, Lobb RR (1986). "Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor". Biochemistry 25 (14): 4097–103. doi:10.1021/bi00362a017. PMID 2427112.
Winkles JA, Friesel R, Burgess WH, et al. (1987). "Human vascular smooth muscle cells both express and respond to heparin-binding growth factor I (endothelial cell growth factor)". Proc. Natl. Acad. Sci. U.S.A. 84 (20): 7124–8. doi:10.1073/pnas.84.20.7124. PMC 299242. PMID 2444975.
Wang WP, Lehtoma K, Varban ML, et al. (1989). "Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues". Mol. Cell. Biol. 9 (6): 2387–95. PMC 362312. PMID 2474753.
Mergia A, Tischer E, Graves D, et al. (1989). "Structural analysis of the gene for human acidic fibroblast growth factor". Biochem. Biophys. Res. Commun. 164 (3): 1121–9. doi:10.1016/0006-291X(89)91785-3. PMID 2590193.
Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (1986). "The complete amino acid sequence of human brain-derived acidic fibroblast growth factor". Biochem. Biophys. Res. Commun. 138 (2): 611–7. doi:10.1016/S0006-291X(86)80540-X. PMID 3527167.
Gautschi P, Fràter-Schröder M, Böhlen P (1986). "Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors". FEBS Lett. 204 (2): 203–7. doi:10.1016/0014-5793(86)80812-2. PMID 3732516.
Gautschi-Sova P, Müller T, Böhlen P (1986). "Amino acid sequence of human acidic fibroblast growth factor". Biochem. Biophys. Res. Commun. 140 (3): 874–80. doi:10.1016/0006-291X(86)90716-3. PMID 3778488.
Gimenez-Gallego G, Conn G, Hatcher VB, Thomas KA (1986). "Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities". Biochem. Biophys. Res. Commun. 135 (2): 541–8. doi:10.1016/0006-291X(86)90028-8. PMID 3964259.
Zhao XM, Yeoh TK, Hiebert M, et al. (1993). "The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells". Transplantation 56 (5): 1177–82. doi:10.1097/00007890-199311000-00025. PMID 7504343.
Pineda-Lucena A, Jiménez MA, Nieto JL, et al. (1994). "1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate". J. Mol. Biol. 242 (1): 81–98. doi:10.1006/jmbi.1994.1558. PMID 7521397.
Chotani MA, Payson RA, Winkles JA, Chiu IM (1995). "Human fibroblast growth factor 1 gene expression in vascular smooth muscle cells is modulated via an alternate promoter in response to serum and phorbol ester". Nucleic Acids Res. 23 (3): 434–41. doi:10.1093/nar/23.3.434. PMC 306694. PMID 7533902.
Opalenik SR, Shin JT, Wehby JN, et al. (1995). "The HIV-1 TAT protein induces the expression and extracellular appearance of acidic fibroblast growth factor". J. Biol. Chem. 270 (29): 17457–67. doi:10.1074/jbc.270.29.17457. PMID 7542239.
Myers RL, Payson RA, Chotani MA, et al. (1993). "Gene structure and differential expression of acidic fibroblast growth factor mRNA: identification and distribution of four different transcripts". Oncogene 8 (2): 341–9. PMID 7678925.

PDB gallery

1afc: STRUCTURAL STUDIES OF THE BINDING OF THE ANTI-ULCER DRUG SUCROSE OCTASULFATE TO ACIDIC FIBROBLAST GROWTH FACTOR

1axm: HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR

1bar: THREE-DIMENSIONAL STRUCTURES OF ACIDIC AND BASIC FIBROBLAST GROWTH FACTORS

1djs: LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR 2 IN COMPLEX WITH FGF1

1dzc: HIGH RESOLUTION STRUCTURE OF ACIDIC FIBROBLAST GROWTH FACTOR. MUTANT FGF-4-ALA-(23-154), 24 NMR STRUCTURES

1dzd: HIGH RESOLUTION STRUCTURE OF ACIDIC FIBROBLAST GROWTH FACTOR (27-154), 24 NMR STRUCTURES

1e0o: CRYSTAL STRUCTURE OF A TERNARY FGF1-FGFR2-HEPARIN COMPLEX

1evt: CRYSTAL STRUCTURE OF FGF1 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1)

1hkn: A COMPLEX BETWEEN ACIDIC FIBROBLAST GROWTH FACTOR AND 5-AMINO-2-NAPHTHALENESULFONATE

1jqz: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag.

1jt3: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Histidine Tag AND LEU 73 REPLACED BY VAL (L73V)

1jt4: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND VAL 109 REPLACED BY LEU (V109L)

1jt5: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L73V/V109L)

1jt7: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE AND LEU 73 REPLACED BY VAL AND VAL 109 REPLACED BY LEU (L44F/L73V/V109L)

1jtc: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag AND LEU 44 REPLACED BY PHE (L44F)

1jy0: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag and Cys 117 replaced with Val (C117V).

1k5u: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with His93 replaced by Gly (H93G).

1k5v: Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag with Asn106 replaced by Gly (N106G).

1m16: Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).

1nzk: Crystal Structure of a Multiple Mutant (L44F, L73V, V109L, L111I, C117V) of Human Acidic Fibroblast Growth Factor

1p63: Human Acidic Fibroblast Growth Factor. 140 Amino Acid Form with Amino Terminal His Tag and Leu111 Replaced with Ile (L111I)

1pzz: Crystal structure of FGF-1, V51N mutant

1q03: Crystal structure of FGF-1, S50G/V51G mutant

1q04: Crystal structure of FGF-1, S50E/V51N

1rg8: Human Acidic Fibroblast Growth Factor (haFGF-1) at 1.10 angstrom resolution (140 amino acid form)

1rml: NMR STUDY OF ACID FIBROBLAST GROWTH FACTOR BOUND TO 1,3,6-NAPHTHALENE TRISULPHONATE, 26 STRUCTURES

1ry7: Crystal Structure of the 3 Ig form of FGFR3c in complex with FGF1

1yto: Crystal Structure of Gly19 deletion Mutant of Human Acidic Fibroblast Growth Factor

1z2v: Crystal Structure of Glu60 deletion Mutant of Human Acidic Fibroblast Growth Factor

1z4s: Crystal Structure of Gly19 and Glu60 deletion mutant of Human Acidic Fibroblast Growth Factor

2afg: 2.0 ANGSTROM X-RAY STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR

2aqz: Crystal structure of FGF-1, S17T/N18T/G19 deletion mutant

2axm: HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST GROWTH FACTOR

2erm: Solution structure of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue

2j3p: CRYSTAL STRUCTURE OF RAT FGF1 AT 1.4 A

v t e Intercellular signaling peptides and proteins / ligands

Growth factors	Endothelial growth factor Epidermal growth factor Fibroblast growth factor Nerve growth factor Platelet-derived growth factor Transforming growth factor beta superfamily

Ephrin	EFNA1 EFNA2 EFNA3 EFNA4 EFNA5 EFNB1 EFNB2 EFNB3

Other	Adipokine Agouti signaling protein Agouti-related protein Angiogenic protein CCN intercellular signaling protein Cysteine-rich protein 61 Connective tissue growth factor Nephroblastoma overexpressed protein Cytokine Endothelin EDN1 EDN2 EDN3 Hedgehog protein Interferon Kinin Parathyroid hormone-related protein Semaphorin Somatomedin Tolloid-like metalloproteinase Tumor necrosis factor Wnt protein

see also extracellular ligand disorders B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

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FGF1

Interactions

See also

References

Further reading