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FGF1 (fibroblast growth factor 1 (acidic))

Written2013-08Seiji Mori, Yoshikazu Takada
Department of Molecular Pathology, Osaka University Graduate School of Medicine, Division of Health Sciences, 1-7 Yamada-oka, Suita-shi, Osaka 565-0871, Japan (SM); Departments of Dermatology, Biochemistry, Molecular Medicine, University of California, Davis School of Medicine, Sacramento, California 95817, USA (YT)

(Note : for Links provided by Atlas : click)

Identity

Alias_namesFGFA
fibroblast growth factor 1 (acidic)
Alias_symbol (synonym)AFGF
ECGF
ECGFA
ECGFB
HBGF1
ECGF-beta
FGF-alpha
GLIO703
Other aliasFGF-1
HBGF-1
HGNC (Hugo) FGF1
LocusID (NCBI) 2246
Atlas_Id 40549
Location 5q31.3  [Link to chromosome band 5q31]
Location_base_pair Starts at 142592178 and ends at 142686495 bp from pter ( according to hg19-Feb_2009)  [Mapping FGF1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
ARHGAP26 (5q31.3) / FGF1 (5q31.3)FGF1 (5q31.3) / C16orf62 (16p12.3)

DNA/RNA

 
  Figure1. FGF1 gene spans 105,89 kb on chromosome 5 in the region of q31.3 on the minus strand. It consists of 3 coding exons and 4 untranslated exons. The transcription is regulated by four distinct promoters. These are separated in the different 5' untranslated exons, designated 1A, 1B, 1C and 1D.
Description The FGF1 gene is located chromosome 5 from 141971743 to 142077617 (105893 bp) on the minus strand.
Transcription The FGF1 gene has 12 splice variants shown in Ensembl database. Nine of transcripts are protein-coding isoforms and 3 of those have no protein product. The FGF1 gene transcript is basically composed of 4 exons and second to fourth exons are protein-coding. The transcription is regulated by at least 4 distinct promoters in different upstream untranslated exons, designated 1A, 1B, 1C, and 1D. These are alternatively spliced to the first protein-coding exon (Chiu et al., 2001). The promoter 1A derived transcript dominantly expresses in the kidney (Myers et al., 1993), 1B in the brain and retina (Myers et al., 1993; Myers et al., 1995), and 1C and 1D in vascular smooth muscle cells and fibroblasts (Chotani et al., 2000).

Protein

 
  Figure 2. Schematic representation of the human FGF1 isoforms.
Description FGFs control multiple biological processes such as proliferation, survival, migration and differentiation of a variety of cell types (Lanner and Rossant, 2010; Guillemot and Zimmer, 2011). The human and mouse FGF family consists of 22 members that are expressed in almost all tissues. Among the FGF family, FGF1 and FGF2 are prototypic FGF and have been extensively characterized. They were originally isolated from the brain and pituitary as mitogens for fibroblast cells in vitro (Gospodarowicz, 1975; Itoh and Ornitz, 2011).
FGF1 contains characteristic β-trefoil structure, since FGF1 contains 12 antiparallel β strands which assemble into a pattern with threefold internal symmetry (Zhu et al., 1991, Brych et al., 2001). Key residues responsible for Interaction between FGF1 and heparin or its receptor are characterized by crystal structure (Pellegrini et al., 2000; Mohammadi et al., 2005a; Mohammadi et al., 2005b).
FGF1 is unique among FGFs because of its ability to bind and activate all known FGFRs, FGF1 is considered to be the universal FGFR ligand (Zhang et al., 2006). Comparison of the crystal structures of FGF1-FGFR1c, FGF1-FGFR2c, and FGF1-FGFR3c complexes has provided key insights into the unique FGFR binding promiscuity of FGF1 (Olsen et al., 2004).
 
  Figure 3. Domaine structure of FGF1. FGF1 contains a nuclear localization signal (NLS) at N-terminal region and heparin binding site is located C-terminal.
Expression Although first isolated from brain and pituitary on the basis of their ability to induce fibroblasts proliferation, FGF1 is widely expressed in developing and adult tissues (Gospodarowicz, 1974; Gospodarowicz, 1975; Gospodarowicz et al., 1978; Itoh and Ornitz, 2004). Immunohistochemical staining has shown that colorectal and gastric tissues, both normal and tumor, express FGF1, and the immunoreactivity is mainly cytoplasmic (el-Hariry et al., 1997). Various amounts of FGF1 are detected in hepatocellular carcinoma, whereas it cannot be detected in normal (Chow et al., 1998). FGF1 mRNA is detected in several types of breast epithelial cell lines such as normal (NMEC), transformed (HBL-100) (Renaud et al., 1996) and cancer cell lines MCF7, BT-20, MDA-MB-231 (Penault-Llorca et al., 1995; Renaud et al., 1996), while BT474, T47D and ZR75.1 do not express FGF1 mRNAs (Penault-Llorca et al., 1995).
 
  Figure 4. Crystal structure of FGF1. Ternary structures are depicted by its crystal structure and representative residues for the binding to its receptor (blue) and heparin (red) are shown.
Localisation FGF1 lacks the classical signal sequence, since it employs non-classical pathway to be secreted. FGF1-S100A13-SYT complex formation is required for passing through the cell membrane (Mouta Carreira et al., 1998; Tarantini et al., 1998; Landriscina et al., 2001). Secreted extracellular FGF1 can be internalized following its binding to cell surface receptors by the clathrin-mediated pathway (Wiedlocha and Sørensen, 2004). FGF1 induces FGF receptor translocation from the cell membrane to the nucleus upon interaction with its receptor during the G1 phase of the fibroblast cell cycle (Prudovsky et al., 1994). FGF1 could be enters the nucleus by its putative nuclear localization sequence (NLS) (Imamura et al., 1990; Rodriguez-Enfedaque et al., 2009). Other groups suggest that nuclear translocation of FGF1 is controled not only by NLS, but also an additional sequence which prevents endogenously expressed FGF1 from NLS dependent translocation to the nucleus, and also FGF1 could move to the nucleus by free diffusion because a molecular weight of FGF1 is only 16500 (Zhan et al., 1992; Cao et al., 1993).
Function FGF1 is a mitogen for numerous different cell types in vitro. FGF1 has been implicated in a range of physiological processes, including development, morphogenesis, wound healing and angiogenesis (Beenken and Mohammadi, 2009). However, FGF1/FGF2 double-knockout mice do not exhibit any of the phenotypic abnormalities. This results suggest that the developmental and physiological roles of FGF1 are highly restricted, even though its functions remain unclear (Miller et al., 2000).
FGF1 binds to integrin ανβ3 (Mori et al., 2008), and the integrin-binding site of FGF1 overlapps with the heparin-binding site (but not identical). The FGF1 mutant that does not bind to ανβ3 (R50E) is dominant-negative (antagonistic), while it still binds to FGFR1 and heparin (Yamaji et al., 2010). FGF1 induces integin-FGF1-FGFR ternary complex, but R50E does not (Yamaji et al., 2010). R50E suppresses angiogenesis and tumorigenesis (Mori et al., 2013).
Homology Length of FGFs is in the range of 150 to 300 amino acids. The conserved core 120-amino acid have been shown a 30-60% identity (Itoh and Ornitz, 2004; Itoh and Ornitz, 2007).

Implicated in

Note
  
Entity Gastrointestinal tumor
Note FGF1 is overexpressed in 42% of colorectal adenomas, 76% of colorectal cancers, and 54% of gastric cancers as compared to the normal mucosal tissues. These results imply that overexpression of FGF1 often arises in a human colorectal and gastric cancers. FGF1 may play a role in the progression of these tumours (el-Hariry et al., 1997). Cancer-associated fibroblasts expressing fibroblast activation protein (FAP) is implicated in the invasive behavior of colorectal cancer. FAP enhances fibroblast cells to produce FGF1 and activates FGFR3 of colon cancer cells in vitro resulted in the increased cell migration and invasion (Henriksson et al., 2011).
  
  
Entity Breast cancer
Note The majority of breast cancer, including cancer adjacent cells expresses active FGF1 protein (Smith et al., 1994); however, mRNA of FGF1 is expressed higher level in benign neoplastic and hyperplastic tissue than in malignant tissue (Anandappa et al., 1994). Another group demonstrates that the extent and intensity of immunoreactivity of FGF1 in cancer cells is much greater than those of cells from fibroadenoma or mastopathy (Yoshimura et al., 1998). FGF1 is detected in epithelial cells of breast fibroadenomas, and FGFR4 is expressed both in epithelial cells and stromal fibroblasts. These suggest a paracrine/autocrine regulation of epithelial and stromal cells of fibroadenomas through an FGF1-FGFR4 interaction (La Rosa et al., 2001).
  
  
Entity Nerve injury
Note FGF1 is one of neuronotrophic factor and enhances nerve regeneration process (Walter et al., 1993). FGF1 increases the branching number of myelinated axons that regenerate damaged neurons and FGF1 also induces the axon elongation of primary sensory and motor neurons through the nerve guide in animals (Cordeiro et al., 1989). Protein expression profiles throughout 28 days of peripheral nerve regeneration reveals that FGF1 increases throughout the experimental period in the both proximal and distal nerve segments (Bryan et al., 2012).
  
  
Entity Cardiac ischemia
Note Level of FGF1 in pericardial fluid is associated with severe myocardial ischemia. FGF1 is released from the myocardial tissue into pericardial result from the myocardial ischemia (Iwakura et al., 2000). FGF1 may contribute to the functional preservation for the myocardium damage. In fact, treatment with FGF1 by extravascular delivery system increases coronary flow in the artificially constricted territory (Lopez et al., 1998), and also systemic bolus of FGF1 immediately after myocardial ischemia reduces apoptosis in animal model (Cuevas et al., 1997).
  

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Citation

This paper should be referenced as such :
Mori, S ; Takada, Y
FGF1 (fibroblast growth factor 1 (acidic))
Atlas Genet Cytogenet Oncol Haematol. 2014;18(3):164-168.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/FGF1ID40549ch5q31.html


External links

Nomenclature
HGNC (Hugo)FGF1   3665
Cards
AtlasFGF1ID40549ch5q31
Entrez_Gene (NCBI)FGF1  2246  fibroblast growth factor 1
AliasesAFGF; ECGF; ECGF-beta; ECGFA; 
ECGFB; FGF-1; FGF-alpha; FGFA; GLIO703; HBGF-1; HBGF1
GeneCards (Weizmann)FGF1
Ensembl hg19 (Hinxton)ENSG00000113578 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000113578 [Gene_View]  chr5:142592178-142686495 [Contig_View]  FGF1 [Vega]
ICGC DataPortalENSG00000113578
TCGA cBioPortalFGF1
AceView (NCBI)FGF1
Genatlas (Paris)FGF1
WikiGenes2246
SOURCE (Princeton)FGF1
Genetics Home Reference (NIH)FGF1
Genomic and cartography
GoldenPath hg38 (UCSC)FGF1  -     chr5:142592178-142686495 -  5q31.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FGF1  -     5q31.3   [Description]    (hg19-Feb_2009)
EnsemblFGF1 - 5q31.3 [CytoView hg19]  FGF1 - 5q31.3 [CytoView hg38]
Mapping of homologs : NCBIFGF1 [Mapview hg19]  FGF1 [Mapview hg38]
OMIM131220   
Gene and transcription
Genbank (Entrez)AI283639 AK289762 AK312301 BC032697 BG706412
RefSeq transcript (Entrez)NM_000800 NM_001144892 NM_001144934 NM_001144935 NM_001257205 NM_001257206 NM_001257207 NM_001257208 NM_001257209 NM_001257210 NM_001257211 NM_001257212 NM_033136 NM_033137
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)FGF1
Cluster EST : UnigeneHs.483635 [ NCBI ]
CGAP (NCI)Hs.483635
Alternative Splicing GalleryENSG00000113578
Gene ExpressionFGF1 [ NCBI-GEO ]   FGF1 [ EBI - ARRAY_EXPRESS ]   FGF1 [ SEEK ]   FGF1 [ MEM ]
Gene Expression Viewer (FireBrowse)FGF1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2246
GTEX Portal (Tissue expression)FGF1
Human Protein AtlasENSG00000113578-FGF1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP05230   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP05230  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP05230
Splice isoforms : SwissVarP05230
PhosPhoSitePlusP05230
Domaine pattern : Prosite (Expaxy)HBGF_FGF (PS00247)   
Domains : Interpro (EBI)FGF1    Fibroblast_GF_fam    IL1/FGF   
Domain families : Pfam (Sanger)FGF (PF00167)   
Domain families : Pfam (NCBI)pfam00167   
Domain families : Smart (EMBL)FGF (SM00442)  
Conserved Domain (NCBI)FGF1
DMDM Disease mutations2246
Blocks (Seattle)FGF1
PDB (SRS)###############################################################################################################################################################################################################################################################   
PDB (PDBSum)###############################################################################################################################################################################################################################################################   
PDB (IMB)###############################################################################################################################################################################################################################################################   
PDB (RSDB)###############################################################################################################################################################################################################################################################   
Structural Biology KnowledgeBase###############################################################################################################################################################################################################################################################   
SCOP (Structural Classification of Proteins)###############################################################################################################################################################################################################################################################   
CATH (Classification of proteins structures)###############################################################################################################################################################################################################################################################   
SuperfamilyP05230
Human Protein Atlas [tissue]ENSG00000113578-FGF1 [tissue]
Peptide AtlasP05230
HPRD00567
IPIIPI00007792   IPI00011866   IPI00383903   IPI00921598   IPI00011868   IPI00942261   IPI00893214   
Protein Interaction databases
DIP (DOE-UCLA)P05230
IntAct (EBI)P05230
FunCoupENSG00000113578
BioGRIDFGF1
STRING (EMBL)FGF1
ZODIACFGF1
Ontologies - Pathways
QuickGOP05230
Ontology : AmiGOMAPK cascade  activation of MAPK activity  angiogenesis  organ induction  protein tyrosine kinase activity  Ras guanyl-nucleotide exchange factor activity  fibroblast growth factor receptor binding  fibroblast growth factor receptor binding  integrin binding  protein binding  extracellular region  extracellular region  proteinaceous extracellular matrix  extracellular space  nucleoplasm  nucleolus  cytosol  cell cortex  signal transduction  multicellular organism development  growth factor activity  heparin binding  heparin binding  cell proliferation  positive regulation of cell proliferation  positive regulation of cell proliferation  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  anatomical structure morphogenesis  positive regulation of endothelial cell migration  regulation of phosphatidylinositol 3-kinase signaling  1-phosphatidylinositol-3-kinase activity  peptidyl-tyrosine phosphorylation  cell differentiation  lung development  positive regulation of cell migration  positive regulation of cell migration  Hsp70 protein binding  activation of protein kinase B activity  cellular response to heat  phosphatidylinositol-3-phosphate biosynthetic process  positive regulation of MAP kinase activity  positive regulation of GTPase activity  S100 protein binding  positive regulation of cholesterol biosynthetic process  positive regulation of angiogenesis  positive regulation of transcription from RNA polymerase II promoter  phosphatidylinositol phosphorylation  phosphatidylinositol-4,5-bisphosphate 3-kinase activity  phosphatidylinositol-mediated signaling  positive regulation of epithelial cell proliferation  positive regulation of cell division  branch elongation involved in ureteric bud branching  positive regulation of ERK1 and ERK2 cascade  mesonephric epithelium development  regulation of endothelial tube morphogenesis  positive regulation of intracellular signal transduction  positive regulation of sprouting angiogenesis  regulation of endothelial cell chemotaxis to fibroblast growth factor  
Ontology : EGO-EBIMAPK cascade  activation of MAPK activity  angiogenesis  organ induction  protein tyrosine kinase activity  Ras guanyl-nucleotide exchange factor activity  fibroblast growth factor receptor binding  fibroblast growth factor receptor binding  integrin binding  protein binding  extracellular region  extracellular region  proteinaceous extracellular matrix  extracellular space  nucleoplasm  nucleolus  cytosol  cell cortex  signal transduction  multicellular organism development  growth factor activity  heparin binding  heparin binding  cell proliferation  positive regulation of cell proliferation  positive regulation of cell proliferation  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  fibroblast growth factor receptor signaling pathway  anatomical structure morphogenesis  positive regulation of endothelial cell migration  regulation of phosphatidylinositol 3-kinase signaling  1-phosphatidylinositol-3-kinase activity  peptidyl-tyrosine phosphorylation  cell differentiation  lung development  positive regulation of cell migration  positive regulation of cell migration  Hsp70 protein binding  activation of protein kinase B activity  cellular response to heat  phosphatidylinositol-3-phosphate biosynthetic process  positive regulation of MAP kinase activity  positive regulation of GTPase activity  S100 protein binding  positive regulation of cholesterol biosynthetic process  positive regulation of angiogenesis  positive regulation of transcription from RNA polymerase II promoter  phosphatidylinositol phosphorylation  phosphatidylinositol-4,5-bisphosphate 3-kinase activity  phosphatidylinositol-mediated signaling  positive regulation of epithelial cell proliferation  positive regulation of cell division  branch elongation involved in ureteric bud branching  positive regulation of ERK1 and ERK2 cascade  mesonephric epithelium development  regulation of endothelial tube morphogenesis  positive regulation of intracellular signal transduction  positive regulation of sprouting angiogenesis  regulation of endothelial cell chemotaxis to fibroblast growth factor  
Pathways : BIOCARTABTG family proteins and cell cycle regulation [Genes]   
Pathways : KEGG   
REACTOMEP05230 [protein]
REACTOME PathwaysR-HSA-8853338 [pathway]   
NDEx NetworkFGF1
Atlas of Cancer Signalling NetworkFGF1
Wikipedia pathwaysFGF1
Orthology - Evolution
OrthoDB2246
GeneTree (enSembl)ENSG00000113578
Phylogenetic Trees/Animal Genes : TreeFamFGF1
HOVERGENP05230
HOGENOMP05230
Homologs : HomoloGeneFGF1
Homology/Alignments : Family Browser (UCSC)FGF1
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerFGF1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)FGF1
dbVarFGF1
ClinVarFGF1
1000_GenomesFGF1 
Exome Variant ServerFGF1
ExAC (Exome Aggregation Consortium)ENSG00000113578
GNOMAD BrowserENSG00000113578
Genetic variants : HAPMAP2246
Genomic Variants (DGV)FGF1 [DGVbeta]
DECIPHERFGF1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisFGF1 
Mutations
ICGC Data PortalFGF1 
TCGA Data PortalFGF1 
Broad Tumor PortalFGF1
OASIS PortalFGF1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICFGF1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDFGF1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch FGF1
DgiDB (Drug Gene Interaction Database)FGF1
DoCM (Curated mutations)FGF1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)FGF1 (select a term)
intoGenFGF1
NCG5 (London)FGF1
Cancer3DFGF1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM131220   
Orphanet
MedgenFGF1
Genetic Testing Registry FGF1
NextProtP05230 [Medical]
TSGene2246
GENETestsFGF1
Target ValidationFGF1
Huge Navigator FGF1 [HugePedia]
snp3D : Map Gene to Disease2246
BioCentury BCIQFGF1
ClinGenFGF1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2246
Chemical/Pharm GKB GenePA28105
Clinical trialFGF1
Miscellaneous
canSAR (ICR)FGF1 (select the gene name)
Probes
Litterature
PubMed201 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineFGF1
EVEXFGF1
GoPubMedFGF1
iHOPFGF1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Thu Oct 12 16:22:15 CEST 2017

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