P05230 (FGF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Cytoplasm › cell cortex. Cytoplasm › cytosol. 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 process	Angiogenesis Differentiation
Cellular component	Cytoplasm Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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 fibroblast growth factor receptor signaling pathway Inferred from direct assay Ref.40. Source: UniProtKB insulin receptor signaling pathway Traceable author statement. Source: Reactome lung development Inferred from electronic annotation. Source: Compara mesonephric epithelium development Inferred from direct assay PubMed 11731227. Source: UniProtKB organ induction Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of intracellular protein kinase cascade Inferred from direct assay PubMed 19229075. Source: BHF-UCL positive regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19229075. Source: BHF-UCL
Cellular_component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 12746488. Source: UniProtKB extracellular space Inferred from direct assay Ref.24. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: Compara proteinaceous extracellular matrix Inferred from electronic annotation. Source: Compara
Molecular_function	growth factor activity Inferred from direct assay Ref.40. Source: UniProtKB heparin binding Inferred from direct assay Ref.40. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FGFR1	P11362	2	EBI-698068,EBI-1028277
FGFR2	P21802	2	EBI-698068,EBI-1028658
FGFR3	P22607	3	EBI-698068,EBI-348399

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Propeptide

2 – 15

14

PRO_0000008907

Chain

16 – 155

140

Fibroblast growth factor 1

PRO_0000008908

Regions

Region

127 – 143

17

Heparin-binding

Motif

24 – 27

4

Nuclear localization signal

Sites

Binding site

33

1

Heparin

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Natural variations

Alternative sequence

57 – 60

4

IQLQ → TDTK in isoform 2.

VSP_036536

Alternative sequence

61 – 155

95

Missing in isoform 2.

VSP_036537

Natural variant

21

1

G → E. Ref.8
Corresponds to variant rs17223632 [ dbSNP | Ensembl ].

VAR_021357

Experimental info

Mutagenesis

24 – 27

4

KKPK → AAPA: Loss of nuclear import leading to loss of phosphorylation by PKC/PRKCD. Ref.28

Mutagenesis

114

1

S → A: Decrease in LRRC59-binding. Ref.22

Mutagenesis

131

1

S → A: Decrease in LRRC59-binding. Ref.22

Mutagenesis

131

1

S → E: Decrease in LRRC59-binding. Ref.22

Mutagenesis

133

1

K → A: Loss of LRRC59-binding. Ref.22

Mutagenesis

133

1

K → E: Loss of CSNK2A-, CSNK2B- and LRRC59-binding. Ref.22

Mutagenesis

133

1

K → R: No effect on LRRC59-binding. Ref.22

Secondary structure

1

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155

Helix Strand Turn

Details...

Turn

11 – 13

3

Beta strand

23 – 25

3

Beta strand

27 – 31

5

Turn

32 – 35

4

Beta strand

36 – 40

5

Turn

42 – 44

3

Beta strand

46 – 49

4

Helix

55 – 57

3

Beta strand

59 – 65

7

Beta strand

68 – 73

6

Turn

74 – 76

3

Beta strand

79 – 82

4

Beta strand

84 – 86

3

Beta strand

88 – 93

6

Helix

96 – 98

3

Beta strand

100 – 105

6

Turn

106 – 108

3

Beta strand

109 – 115

7

Helix

118 – 120

3

Beta strand

130 – 132

3

Helix

135 – 137

3

Turn

138 – 141

4

Helix

143 – 145

3

Beta strand

147 – 151

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: F586E8BFB09F1580	FASTA	155	17,460
	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
	Isoform 2 [UniParc]. Checksum: B53E08C406484714	FASTA	60	6,698
	10 20 30 40 50 60 MAEGEITTFT ALTEKFNLPP GNYKKPKLLY CSNGGHFLRI LPDGTVDGTR DRSDQHTDTK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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

NIEHS-SNPs

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.

IPI

IPI00007792.
IPI00011866.

PIR

A33665.
JH0708.

RefSeq

NP_000791.1. NM_000800.4.
NP_001138364.1. NM_001144892.2.
NP_001138406.1. NM_001144934.1.
NP_001138407.1. NM_001144935.1.
NP_001244134.1. NM_001257205.1.
NP_001244136.1. NM_001257207.1.
NP_001244137.1. NM_001257208.1.
NP_001244138.1. NM_001257209.1.
NP_001244139.1. NM_001257210.1.
NP_149127.1. NM_033136.3.
NP_149128.1. NM_033137.2.

UniGene

Hs.483635.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AXM	X-ray	3.00	A/B/C/D/E/F	21-155	[»]
1DJS	X-ray	2.40	B	21-155	[»]
1DZC	NMR	-	A	28-155	[»]
1DZD	NMR	-	A	29-155	[»]
1E0O	X-ray	2.80	A/C	16-155	[»]
1EVT	X-ray	2.80	A/B	22-155	[»]
1HKN	X-ray	2.00	A/B/C/D/E/F	17-155	[»]
1JQZ	X-ray	1.65	A/B	16-155	[»]
1JT3	X-ray	1.95	A/B	16-155	[»]
1JT4	X-ray	1.78	A/B	16-155	[»]
1JT5	X-ray	1.85	A/B	16-155	[»]
1JT7	X-ray	1.70	A/B/C/D	16-155	[»]
1JTC	X-ray	1.70	A/B/C/D	16-155	[»]
1JY0	X-ray	1.70	A/B	16-155	[»]
1K5U	X-ray	2.00	A/B/C	16-155	[»]
1K5V	X-ray	2.10	A/B	16-155	[»]
1M16	X-ray	1.70	A/B	16-155	[»]
1NZK	X-ray	1.95	A/B/C/D	16-152	[»]
1P63	X-ray	1.60	A/B	16-155	[»]
1PZZ	X-ray	2.00	A/B	16-155	[»]
1Q03	X-ray	2.05	A/B	16-152	[»]
1Q04	X-ray	1.80	A/B	16-155	[»]
1QCT	model	-	A/D	24-153	[»]
1RG8	X-ray	1.10	A/B	16-155	[»]
1RML	NMR	-	A	1-155	[»]
1RY7	X-ray	3.20	A	1-155	[»]
1YTO	X-ray	2.10	A/B/C/D	16-155	[»]
1Z2V	X-ray	1.90	A/B	16-155	[»]
1Z4S	X-ray	2.60	A/B/C/D	16-155	[»]
2AFG	X-ray	2.00	A/B/C/D	16-155	[»]
2AQZ	X-ray	1.85	A/B	16-155	[»]
2AXM	X-ray	3.00	A/B	21-155	[»]
2ERM	NMR	-	A	17-155	[»]
2HW9	X-ray	1.60	A/B	16-155	[»]
2HWA	X-ray	1.65	A/B	16-155	[»]
2HWM	X-ray	1.60	A/B	16-155	[»]
2HZ9	X-ray	1.70	A/B	16-155	[»]
2K43	NMR	-	A	23-155	[»]
2K4A	NMR	-	B	23-155	[»]
2K8R	NMR	-	A	23-155	[»]
2KI4	NMR	-	A/D	23-155	[»]
2KI6	NMR	-	B/E	23-155	[»]
2LDN	NMR	-	A	23-152	[»]
2NTD	X-ray	2.52	A/B/C/D	16-155	[»]
2Q9X	X-ray	1.70	A	16-155	[»]
2RQ9	NMR	-	A	22-155	[»]
3B9U	X-ray	1.55	A	16-155	[»]
3BA4	X-ray	1.80	A/B	16-155	[»]
3BA5	X-ray	1.75	A/B	16-155	[»]
3BA7	X-ray	1.60	A/B	16-155	[»]
3BAD	X-ray	2.00	A/B	16-155	[»]
3BAG	X-ray	1.75	A/B	16-155	[»]
3BAH	X-ray	1.65	A/B	16-155	[»]
3BAO	X-ray	1.55	A/B	16-155	[»]
3BAQ	X-ray	1.80	A/B	16-155	[»]
3BAU	X-ray	1.60	A/B	16-155	[»]
3BAV	X-ray	1.62	A/B	16-155	[»]
3BB2	X-ray	1.50	A/B	16-155	[»]
3CQA	X-ray	1.80	A/B	16-155	[»]
3CRG	X-ray	1.85	A/B	16-155	[»]
3CRH	X-ray	2.15	A/B	16-155	[»]
3CRI	X-ray	2.10	A/B	16-155	[»]
3CU1	X-ray	2.60	B/D	22-152	[»]
3FGM	X-ray	1.95	A/B	16-155	[»]
3FJ8	X-ray	2.00	A/B	16-155	[»]
3FJ9	X-ray	1.90	A/B	16-155	[»]
3FJA	X-ray	1.95	A/B	16-155	[»]
3FJB	X-ray	2.00	A/B	16-155	[»]
3FJC	X-ray	2.00	A/B	16-155	[»]
3FJD	X-ray	1.90	A/B	16-155	[»]
3FJE	X-ray	2.10	A/B	16-155	[»]
3FJF	X-ray	1.90	A/B	16-155	[»]
3FJH	X-ray	1.90	A/B	16-155	[»]
3FJI	X-ray	2.55	A/B/C/D	16-155	[»]
3FJJ	X-ray	1.90	A/B	16-155	[»]
3FJK	X-ray	2.15	A/B/C/D	16-155	[»]
3HOM	X-ray	2.30	A/B	16-155	[»]
3JUT	X-ray	2.25	A/B/C/D/E/F	24-153	[»]
3K1X	X-ray	1.98	A/B/C/D/E/F	24-153	[»]
3O3Q	X-ray	1.60	A/B/C/D	16-155	[»]
3OJ2	X-ray	2.20	A/B	1-155	[»]
3OJM	X-ray	2.10	A	1-155	[»]
3OJV	X-ray	2.60	A/B	21-155	[»]
3UD7	X-ray	2.80	A/B/C	16-155	[»]
3UD8	X-ray	2.37	A/B/C	16-155	[»]
3UD9	X-ray	2.34	A/B/C	16-155	[»]
3UDA	X-ray	2.51	A/B/C	16-155	[»]

ProteinModelPortal

P05230.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3787N.

IntAct

P05230. 4 interactions.

MINT

MINT-118570.

STRING

9606.ENSP00000338548.

Polymorphism databases

DMDM

122737.

Proteomic databases

PaxDb

P05230.

PRIDE

P05230.

Protocols and materials databases

DNASU

2246.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337706; ENSP00000338548; ENSG00000113578.
ENST00000359370; ENSP00000352329; ENSG00000113578.
ENST00000360966; ENSP00000354231; ENSG00000113578.
ENST00000378046; ENSP00000367285; ENSG00000113578.
ENST00000419524; ENSP00000396195; ENSG00000113578.
ENST00000441680; ENSP00000404742; ENSG00000113578.

GeneID

2246.

KEGG

hsa:2246.

UCSC

uc003lmm.3. human.
uc003lmp.4. human.

Organism-specific databases

CTD

2246.

GeneCards

GC05M141953.

HGNC

HGNC:3665. FGF1.

HPA

CAB017519.
HPA003265.

MIM

131220. gene.

neXtProt

NX_P05230.

PharmGKB

PA28105.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG246422.

HOGENOM

HOG000236341.

HOVERGEN

HBG007580.

InParanoid

P05230.

KO

K04358.

OMA

PSEECLF.

OrthoDB

EOG48KRCM.

PhylomeDB

P05230.

Enzyme and pathway databases

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P05230.

Bgee

P05230.

CleanEx

HS_FGF1.

Genevestigator

P05230.

GermOnline

ENSG00000113578. Homo sapiens.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR002209. GF_heparin-bd.
IPR002348. IL1_HBGF.
[Graphical view]

PANTHER

PTHR11486. PTHR11486. 1 hit.

Pfam

PF00167. FGF. 1 hit.
[Graphical view]

PRINTS

PR00263. HBGFFGF.
PR00262. IL1HBGF.

SMART

SM00442. FGF. 1 hit.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05230.

ChEMBL

CHEMBL2120.

ChiTaRS

FGF1. human.

DrugBank

DB00686. Pentosan Polysulfate.

EvolutionaryTrace

P05230.

GenomeRNAi

2246.

NextBio

9087.

SOURCE

Search...

Entry information

Entry name

FGF1_HUMAN

Accession

Primary (citable) accession number: P05230
Secondary accession number(s): B2R5T0 , D3DQF2, P07502, Q16588

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 167 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.