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P05230 (FGF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 181. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor 1

Short name=FGF-1
Alternative name(s):
Acidic fibroblast growth factor
Short name=aFGF
Endothelial cell growth factor
Short name=ECGF
Heparin-binding growth factor 1
Short name=HBGF-1
Gene names
Name:FGF1
Synonyms:FGFA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.20 Ref.23 Ref.40

Subunit structure

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. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP1. Part of a Cu2+-dependent multiprotein aggregate containing FGF1, S100A13 and SYT1. Interacts with SYT1 By similarity. Interacts with S100A13. Interacts with LRRC59. Interacts with CSNKA, CSNKB and FIBP. While binding with LRRC59, CSNKA and FIBP seem mutually exclusive, CSNKB and FIBP may cooperatively interact with FGF1. Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.40

Subcellular location

Secreted. Cytoplasm. Cytoplasmcell cortex. Cytoplasmcytosol. Nucleus. Note: Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu2+ ions and S100A13. Secreted in a complex with SYT1 By similarity. Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 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 LRRC59. Ref.21 Ref.22 Ref.24 Ref.25 Ref.28

Tissue specificity

Predominantly expressed in kidney and brain. Detected at much lower levels in heart and skeletal muscle. Ref.7 Ref.22

Post-translational modification

In the nucleus, phosphorylated by PKC/PRKCD. Ref.28

Sequence similarities

Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentCytoplasm
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandHeparin-binding
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

anatomical structure morphogenesis

Traceable author statement Ref.4. Source: ProtInc

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

branch elongation involved in ureteric bud branching

Inferred from direct assay PubMed 11731227. Source: UniProtKB

cellular response to heat

Inferred from direct assay PubMed 12746488. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Inferred from direct assay Ref.40. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

mesonephric epithelium development

Inferred from direct assay PubMed 11731227. Source: UniProtKB

multicellular organismal development

Traceable author statement PubMed 10903182. Source: ProtInc

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

organ induction

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of angiogenesis

Inferred from direct assay Ref.40. Source: UniProtKB

positive regulation of cell division

Inferred from direct assay Ref.40. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay Ref.40. Source: UniProtKB

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 18187602Ref.20. Source: MGI

positive regulation of cholesterol biosynthetic process

Inferred from direct assay PubMed 19229075. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular signal transduction

Inferred from direct assay PubMed 19229075. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19229075. Source: BHF-UCL

signal transduction

Non-traceable author statement Ref.16. Source: ProtInc

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay PubMed 12746488. Source: UniProtKB

extracellular region

Inferred from direct assay PubMed 12746488. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.24. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionS100 protein binding

Inferred from physical interaction Ref.21. Source: UniProtKB

fibroblast growth factor receptor binding

Inferred from physical interaction Ref.32PubMed 12815063. Source: MGI

growth factor activity

Inferred from direct assay Ref.40. Source: UniProtKB

heparin binding

Inferred from direct assay Ref.40. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.34Ref.32Ref.33Ref.36PubMed 18441324PubMed 23597563. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05230-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05230-2)

The sequence of this isoform differs from the canonical sequence as follows:
     57-60: IQLQ → TDTK
     61-155: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Propeptide2 – 1514
PRO_0000008907
Chain16 – 155140Fibroblast growth factor 1
PRO_0000008908

Regions

Region127 – 14317Heparin-binding
Motif24 – 274Nuclear localization signal

Sites

Binding site331Heparin

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence57 – 604IQLQ → TDTK in isoform 2.
VSP_036536
Alternative sequence61 – 15595Missing in isoform 2.
VSP_036537
Natural variant211G → E. Ref.8
Corresponds to variant rs17223632 [ dbSNP | Ensembl ].
VAR_021357

Experimental info

Mutagenesis24 – 274KKPK → AAPA: Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD. Ref.28
Mutagenesis1141S → A: Decrease in LRRC59-binding. Ref.22
Mutagenesis1311S → A: Decrease in LRRC59-binding. Ref.22
Mutagenesis1311S → E: Decrease in LRRC59-binding. Ref.22
Mutagenesis1331K → A: Loss of LRRC59-binding. Ref.22
Mutagenesis1331K → E: Loss of CSNK2A-, CSNK2B- and LRRC59-binding. Ref.22
Mutagenesis1331K → R: No effect on LRRC59-binding. Ref.22

Secondary structure

............................................. 155
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: F586E8BFB09F1580

FASTA15517,460
        10         20         30         40         50         60 
MAEGEITTFT ALTEKFNLPP GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR DRSDQHIQLQ 

        70         80         90        100        110        120 
LSAESVGEVY IKSTETGQYL AMDTDGLLYG SQTPNEECLF LERLEENHYN TYISKKHAEK 

       130        140        150 
NWFVGLKKNG SCKRGPRTHY GQKAILFLPL PVSSD 

« Hide

Isoform 2 [UniParc].

Checksum: B53E08C406484714
Show »

FASTA606,698

References

« Hide 'large scale' references
[1]"Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization."
Jaye M., Howk R., Burgess W., Ricca G.A., Chiu I.-M., Ravera M.W., O'Brien S.J., Modi W.S., Maciag T., Drohan W.N.
Science 233:541-545(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain stem.
[2]"Structural analysis of the gene for human acidic fibroblast growth factor."
Mergia A., Tischer E., Graves D., Tumolo A., Miller J., Gospodarowicz D., Abraham J.A., Shipley G.D., Fiddes J.C.
Biochem. Biophys. Res. Commun. 164:1121-1129(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues."
Wang W.P., Lehtoma K., Varban M.L., Krishnan I., Chiu I.M.
Mol. Cell. Biol. 9:2387-2395(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain stem.
[4]"Alternative splicing generates two forms of mRNA coding for human heparin-binding growth factor 1."
Chiu I.M., Wang W.P., Lehtoma K.
Oncogene 5:755-762(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain stem.
[5]"Cloning and sequence analysis of the human acidic fibroblast growth factor gene and its preservation in leukemia patients."
Wang W.P., Quick D., Balcerzak S.P., Needleman S.W., Chiu I.M.
Oncogene 6:1521-1529(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"An acidic fibroblast growth factor protein generated by alternate splicing acts like an antagonist."
Li Y.L., Kha H., Golden J.A., Migchielsen A.A.J., Goetzl E.J., Turck E.J.
J. Exp. Med. 175:1073-1080(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]"The expression of acidic fibroblast growth factor (heparin-binding growth factor-1) and cytokine genes in human cardiac allografts and T cells."
Zhao X.M., Yeoh T.K., Hiebert M., Frist W.H., Miller G.G.
Transplantation 56:1177-1182(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-154 (ISOFORM 1), TISSUE SPECIFICITY.
[8]NIEHS SNPs program
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-21.
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cerebellum.
[10]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Liver.
[13]"The gene for human acidic fibroblast growth factor encodes two upstream exons alternatively spliced to the first coding exon."
Crumley G., Dionne C.A., Jaye M.
Biochem. Biophys. Res. Commun. 171:7-13(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-40 (ISOFORMS 1/2).
[14]"Human class 1 heparin-binding growth factor: structure and homology to bovine acidic brain fibroblast growth factor."
Harper J.W., Strydom D.J., Lobb R.R.
Biochemistry 25:4097-4103(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
[15]"The complete amino acid sequence of human brain-derived acidic fibroblast growth factor."
Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.
Biochem. Biophys. Res. Commun. 138:611-617(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
[16]"Amino acid sequence of human acidic fibroblast growth factor."
Gautschi-Sova P., Mueller T., Boehlen P.
Biochem. Biophys. Res. Commun. 140:874-880(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-155 (ISOFORM 1).
[17]"Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities."
Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.
Biochem. Biophys. Res. Commun. 135:541-548(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-47 (ISOFORMS 1/2).
[18]"Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors."
Gautschi P., Frater-Schroeder M., Boehlen P.
FEBS Lett. 204:203-207(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-49 (ISOFORMS 1/2).
[19]"Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors."
Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.
J. Biol. Chem. 266:16778-16785(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF2, INTERACTION WITH FGFBP1.
[20]"Receptor specificity of the fibroblast growth factor family."
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., Gao G., Goldfarb M.
J. Biol. Chem. 271:15292-15297(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN CELL PROLIFERATION.
[21]"Copper induces the assembly of a multiprotein aggregate implicated in the release of fibroblast growth factor 1 in response to stress."
Landriscina M., Bagala C., Mandinova A., Soldi R., Micucci I., Bellum S., Prudovsky I., Maciag T.
J. Biol. Chem. 276:25549-25557(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, COPPER-BINDING, INTERACTION WITH S100A13 AND SYT1.
[22]"Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor."
Skjerpen C.S., Wesche J., Olsnes S.
J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSNK2A; CSNK2B; FGF2; FIBP AND LRRC59, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-114; SER-131 AND LYS-133.
[23]"Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family."
Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M.
J. Biol. Chem. 281:15694-15700(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
[24]"The release of fibroblast growth factor-1 from melanoma cells requires copper ions and is mediated by phosphatidylinositol 3-kinase/Akt intracellular signaling pathway."
Di Serio C., Doria L., Pellerito S., Prudovsky I., Micucci I., Massi D., Landriscina M., Marchionni N., Masotti G., Tarantini F.
Cancer Lett. 267:67-74(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[25]"Effect of human S100A13 gene silencing on FGF-1 transportation in human endothelial cells."
Cao R., Yan B., Yang H., Zu X., Wen G., Zhong J.
J. Formos. Med. Assoc. 109:632-640(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[26]"Cellular signaling by fibroblast growth factor receptors."
Eswarakumar V.P., Lax I., Schlessinger J.
Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[27]"Fibroblast growth factor signalling: from development to cancer."
Turner N., Grose R.
Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[28]"Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnalpha1 and Kpnbeta1."
Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y., Walchli S., Olsnes S., Wiedlocha A.
Traffic 13:650-664(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF 24-LYS--LYS-27.
[29]"Three-dimensional structures of acidic and basic fibroblast growth factors."
Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C.
Science 251:90-93(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-155.
[30]"X-ray crystal structure of human acidic fibroblast growth factor."
Blaber M., Disalvo J., Thomas K.A.
Biochemistry 35:2086-2094(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-155.
[31]"Structure of a heparin-linked biologically active dimer of fibroblast growth factor."
DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M., Schlessinger J., Hendrickson W.A.
Nature 393:812-817(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-155 IN COMPLEX WITH HEPARIN.
[32]"Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity."
Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.
Cell 101:413-424(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-155 IN COMPLEX WITH FGFR1.
[33]"Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin."
Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.
Nature 407:1029-1034(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-155 IN COMPLEX WITH FGFR2 AND HEPARIN.
[34]"Structural interactions of fibroblast growth factor receptor with its ligands."
Stauber D.J., DiGabriele A.D., Hendrickson W.A.
Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-155 IN COMPLEX WITH FGFR2.
[35]"Alternative type I and I' turn conformations in the beta8/beta9 beta-hairpin of human acidic fibroblast growth factor."
Kim J., Blaber S.I., Blaber M.
Protein Sci. 11:459-466(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-155.
[36]"Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity."
Olsen S.K., Ibrahimi O.A., Raucci A., Zhang F., Eliseenkova A.V., Yayon A., Basilico C., Linhardt R.J., Schlessinger J., Mohammadi M.
Proc. Natl. Acad. Sci. U.S.A. 101:935-940(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FGFR3.
[37]"1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate."
Pineda-Lucena A., Jimenez M.A., Nieto J.L., Santoro J., Rico M., Gimenez-Gallego G.
J. Mol. Biol. 242:81-98(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-155 IN COMPLEX WITH INOSITOL HEXASULFATE, PROTEIN SEQUENCE OF 24-27.
[38]"Three-dimensional structure of acidic fibroblast growth factor in solution: effects of binding to a heparin functional analog."
Pineda-Lucena A., Jimenez M.A., Lozano R.M., Nieto J.L., Santoro J., Rico M., Gimenez-Gallego G.
J. Mol. Biol. 264:162-178(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-155.
[39]"Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas."
Lozano R.M., Jimenez M., Santoro J., Rico M., Gimenez-Gallego G.
J. Mol. Biol. 281:899-915(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-155.
[40]"Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors."
Fernandez I.S., Cuevas P., Angulo J., Lopez-Navajas P., Canales-Mayordomo A., Gonzalez-Corrochano R., Lozano R.M., Valverde S., Jimenez-Barbero J., Romero A., Gimenez-Gallego G.
J. Biol. Chem. 285:11714-11729(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 24-153 IN COMPLEX WITH GENTISIC ACID AND 2,5-DIHYDROXYPHENYLSULFONATE, FUNCTION, HEPARIN-BINDING, INTERACTION WITH WITH FGFR1.
[41]"The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion."
Mohan S.K., Rani S.G., Yu C.
J. Biol. Chem. 285:15464-15475(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 23-155.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13361 mRNA. Translation: AAA79245.1.
M30492, M30490, M30491 Genomic DNA. Translation: AAA52446.1.
M23087, M23086 Genomic DNA. Translation: AAA52638.1.
X51943 mRNA. Translation: CAA36206.1.
X65778 mRNA. Translation: CAA46661.1.
S67291 mRNA. Translation: AAB29057.2.
S67292 mRNA. Translation: AAB29058.1.
AY601819 Genomic DNA. Translation: AAS99352.1.
AC005370 Genomic DNA. No translation available.
AK312301 mRNA. Translation: BAG35227.1.
CH471062 Genomic DNA. Translation: EAW61881.1.
CH471062 Genomic DNA. Translation: EAW61882.1.
CH471062 Genomic DNA. Translation: EAW61885.1.
BC032697 mRNA. Translation: AAH32697.1.
M60515 mRNA. Translation: AAA51672.1.
M60516 mRNA. Translation: AAA51673.1.
CCDSCCDS4275.1. [P05230-1]
CCDS4276.1. [P05230-2]
PIRA33665.
JH0708.
RefSeqNP_000791.1. NM_000800.4. [P05230-1]
NP_001138364.1. NM_001144892.2. [P05230-1]
NP_001138406.1. NM_001144934.1. [P05230-1]
NP_001138407.1. NM_001144935.1. [P05230-1]
NP_001244134.1. NM_001257205.1. [P05230-1]
NP_001244136.1. NM_001257207.1. [P05230-1]
NP_001244137.1. NM_001257208.1. [P05230-1]
NP_001244138.1. NM_001257209.1. [P05230-1]
NP_001244139.1. NM_001257210.1. [P05230-1]
NP_149127.1. NM_033136.3. [P05230-2]
NP_149128.1. NM_033137.2.
UniGeneHs.483635.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AXMX-ray3.00A/B/C/D/E/F21-155[»]
1DJSX-ray2.40B21-155[»]
1DZCNMR-A25-155[»]
1DZDNMR-A29-155[»]
1E0OX-ray2.80A/C16-155[»]
1EVTX-ray2.80A/B22-155[»]
1HKNX-ray2.00A/B/C/D/E/F17-155[»]
1JQZX-ray1.65A/B16-155[»]
1JT3X-ray1.95A/B16-155[»]
1JT4X-ray1.78A/B16-155[»]
1JT5X-ray1.85A/B16-155[»]
1JT7X-ray1.70A/B/C/D16-155[»]
1JTCX-ray1.70A/B/C/D16-155[»]
1JY0X-ray1.70A/B16-155[»]
1K5UX-ray2.00A/B/C16-154[»]
1K5VX-ray2.10A/B16-154[»]
1M16X-ray1.70A/B16-155[»]
1NZKX-ray1.95A/B/C/D16-152[»]
1P63X-ray1.60A/B16-155[»]
1PZZX-ray2.00A/B16-155[»]
1Q03X-ray2.05A/B16-152[»]
1Q04X-ray1.80A/B16-155[»]
1QCTmodel-A/D24-153[»]
1RG8X-ray1.10A/B16-155[»]
1RMLNMR-A1-155[»]
1RY7X-ray3.20A1-155[»]
1YTOX-ray2.10A/B/C/D16-155[»]
1Z2VX-ray1.90A/B16-155[»]
1Z4SX-ray2.60A/B/C/D16-155[»]
2AFGX-ray2.00A/B/C/D16-155[»]
2AQZX-ray1.85A/B16-155[»]
2AXMX-ray3.00A/B21-155[»]
2ERMNMR-A17-155[»]
2HW9X-ray1.60A/B16-155[»]
2HWAX-ray1.65A/B16-155[»]
2HWMX-ray1.60A/B16-155[»]
2HZ9X-ray1.70A/B16-155[»]
2K43NMR-A23-155[»]
2K4ANMR-B23-155[»]
2K8RNMR-A23-155[»]
2KI4NMR-A/D23-155[»]
2KI6NMR-B/E23-155[»]
2LDNNMR-A23-152[»]
2NTDX-ray2.52A/B/C/D16-155[»]
2Q9XX-ray1.70A16-155[»]
2RQ9NMR-A22-155[»]
3B9UX-ray1.55A16-155[»]
3BA4X-ray1.80A/B16-155[»]
3BA5X-ray1.75A/B16-155[»]
3BA7X-ray1.60A/B16-155[»]
3BADX-ray2.00A/B16-155[»]
3BAGX-ray1.75A/B16-155[»]
3BAHX-ray1.65A/B16-155[»]
3BAOX-ray1.55A/B16-155[»]
3BAQX-ray1.80A/B16-155[»]
3BAUX-ray1.60A/B16-155[»]
3BAVX-ray1.62A/B16-155[»]
3BB2X-ray1.50A/B16-155[»]
3CQAX-ray1.80A/B16-155[»]
3CRGX-ray1.85A/B16-155[»]
3CRHX-ray2.15A/B16-155[»]
3CRIX-ray2.10A/B16-155[»]
3CU1X-ray2.60B/D22-152[»]
3FGMX-ray1.95A/B16-155[»]
3FJ8X-ray2.00A/B16-155[»]
3FJ9X-ray1.90A/B16-155[»]
3FJAX-ray1.95A/B16-155[»]
3FJBX-ray2.00A/B16-155[»]
3FJCX-ray2.00A/B16-155[»]
3FJDX-ray1.90A/B16-155[»]
3FJEX-ray2.10A/B16-155[»]
3FJFX-ray1.90A/B16-155[»]
3FJHX-ray1.90A/B16-155[»]
3FJIX-ray2.55A/B/C/D16-155[»]
3FJJX-ray1.90A/B16-155[»]
3FJKX-ray2.15A/B/C/D16-155[»]
3HOMX-ray2.30A/B16-155[»]
3JUTX-ray2.25A/B/C/D/E/F24-153[»]
3K1XX-ray1.98A/B/C/D/E/F24-153[»]
3O3QX-ray1.60A/B/C/D16-155[»]
3OJ2X-ray2.20A/B1-155[»]
3OJMX-ray2.10A1-155[»]
3OJVX-ray2.60A/B21-155[»]
3UD7X-ray2.80A/B/C16-155[»]
3UD8X-ray2.37A/B/C16-155[»]
3UD9X-ray2.34A/B/C16-155[»]
3UDAX-ray2.51A/B/C16-155[»]
4J23X-ray3.88B21-155[»]
ProteinModelPortalP05230.
SMRP05230. Positions 16-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108537. 14 interactions.
DIPDIP-3787N.
IntActP05230. 5 interactions.
MINTMINT-118570.
STRING9606.ENSP00000338548.

Chemistry

BindingDBP05230.
ChEMBLCHEMBL2120.
DrugBankDB00686. Pentosan Polysulfate.

Polymorphism databases

DMDM122737.

Proteomic databases

MaxQBP05230.
PaxDbP05230.
PRIDEP05230.

Protocols and materials databases

DNASU2246.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337706; ENSP00000338548; ENSG00000113578. [P05230-1]
ENST00000359370; ENSP00000352329; ENSG00000113578. [P05230-1]
ENST00000360966; ENSP00000354231; ENSG00000113578. [P05230-2]
ENST00000378046; ENSP00000367285; ENSG00000113578. [P05230-1]
ENST00000419524; ENSP00000396195; ENSG00000113578. [P05230-1]
ENST00000441680; ENSP00000404742; ENSG00000113578. [P05230-1]
GeneID2246.
KEGGhsa:2246.
UCSCuc003lmm.4. human. [P05230-1]
uc003lmp.5. human. [P05230-2]

Organism-specific databases

CTD2246.
GeneCardsGC05M141953.
HGNCHGNC:3665. FGF1.
HPACAB017519.
HPA003265.
MIM131220. gene.
neXtProtNX_P05230.
PharmGKBPA28105.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246422.
HOGENOMHOG000236341.
HOVERGENHBG007580.
InParanoidP05230.
KOK04358.
OMANGLLYGS.
OrthoDBEOG7992S1.
PhylomeDBP05230.
TreeFamTF317805.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP05230.

Gene expression databases

ArrayExpressP05230.
BgeeP05230.
CleanExHS_FGF1.
GenevestigatorP05230.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR028210. FGF1.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF65. PTHR11486:SF65. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
PRINTSPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGF1. human.
EvolutionaryTraceP05230.
GeneWikiFGF1.
GenomeRNAi2246.
NextBio9087.
PROP05230.
SOURCESearch...

Entry information

Entry nameFGF1_HUMAN
AccessionPrimary (citable) accession number: P05230
Secondary accession number(s): B2R5T0 expand/collapse secondary AC list , D3DQF2, P07502, Q16588
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: July 9, 2014
This is version 181 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM