Reviewed, UniProtKB/Swiss-Prot P05230 (FGF1_HUMAN)

Names and origin

Protein names

Recommended name:
    Heparin-binding growth factor 1
      Short name=HBGF-1
Alternative name(s):
    Acidic fibroblast growth factor
      Short name=aFGF
    Beta-endothelial cell growth factor
    ECGF-beta

Gene names

Name:	FGF1
Synonyms:	FGFA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
Subunit structure	Monomer. Binds FGFR2. Forms a ternary complex containing 2 molecules each of FGFR2 and FGF1 for 1 heparin molecule. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP1. Ref.19
Miscellaneous	This protein binds heparin, although less strongly than does bFGF.
Sequence similarities	Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cellular response to heat Inferred from direct assay. Source: UniProtKB fibroblast growth factor receptor signaling pathway Ref.23 Inferred from genetic interaction. Source: MGI positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	fibroblast growth factor receptor binding Ref.23 Inferred from physical interaction. Source: MGI growth factor activity Ref.4 Traceable author statement. Source: ProtInc heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FGFR2	P21802	1	EBI-698068,EBI-1028658
FGFR3	P22607	2	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

Propeptide

1 – 15

15

PRO_0000008907

Chain

16 – 155

140

Heparin-binding growth factor 1

PRO_0000008908

Regions

Region

127 – 143

17

Heparin-binding

Sites

Binding site

33

1

Heparin

Amino acid modifications

Modified residue

2

1

N-acetylalanine

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: dbSNP rs17223632. Ref.8

VAR_021357

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

Beta strand

46 – 49

4

Beta strand

59 – 65

7

Beta strand

68 – 73

6

Turn

74 – 76

3

Beta strand

79 – 82

4

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

Helix

135 – 137

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. 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: 3523756] [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: 2590193] [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: 2474753] [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: 1693186] [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: 1717925] [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: 1372643] [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: 7504343] [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: 14702039] [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: 15372022] [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: 15489334] [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: 2393407] [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: 2427112] [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: 3527167] [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: 3778488] [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: 3964259] [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: 3732516] [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: 1885605] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF2, INTERACTION WITH FGFBP1.
[20]	"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: 1702556] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 16-155.
[21]	"X-ray crystal structure of human acidic fibroblast growth factor." Blaber M., Disalvo J., Thomas K.A. Biochemistry 35:2086-2094(1996) [PubMed: 8652550] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-155.
[22]	"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: 9655399] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-155 IN COMPLEX WITH HEPARIN.
[23]	"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: 10830168] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-155 IN COMPLEX WITH FGFR1.
[24]	"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: 11069186] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 16-155 IN COMPLEX WITH FGFR2 AND HEPARIN.
[25]	"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: 10618369] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-155 IN COMPLEX WITH FGFR2.
[26]	"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: 11847269] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-155.
[27]	"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: 14732692] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH FGFR3.
[28]	"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: 7521397] [Abstract] Cited for: STRUCTURE BY NMR OF 24-155 IN COMPLEX WITH INOSITOL HEXASULFATE, PROTEIN SEQUENCE OF 24-27.
[29]	"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: 8950275] [Abstract] Cited for: STRUCTURE BY NMR OF 24-155.
[30]	"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: 9719643] [Abstract] Cited for: STRUCTURE BY NMR OF 24-155.
+	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.
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.
NP_001138364.1.
NP_001138406.1.
NP_001138407.1.
NP_149127.1.
NP_149128.1.

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	[»]
2NTD	X-ray	2.52	A/B/C/D	16-155	[»]
2Q9X	X-ray	1.70	A	16-155	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3787N.

IntAct

P05230. 2 interactions.

STRING

P05230.

PTM databases

PhosphoSite

P05230.

Proteomic databases

PRIDE

P05230.

Genome annotation databases

Ensembl

ENST00000337706; ENSP00000338548; ENSG00000113578; Homo sapiens. [Genome view]
ENST00000359370; ENSP00000352329; ENSG00000113578; Homo sapiens. [Genome view]
ENST00000378046; ENSP00000367285; ENSG00000113578; Homo sapiens. [Genome view]
ENST00000403113; ENSP00000384502; ENSG00000113578; Homo sapiens. [Genome view]
ENST00000419524; ENSP00000396195; ENSG00000113578; Homo sapiens. [Genome view]
ENST00000441680; ENSP00000404742; ENSG00000113578; Homo sapiens. [Genome view]

GeneID

2246.

KEGG

hsa:2246.

UCSC

uc003lmm.1. human.

Organism-specific databases

CTD

2246.

GeneCards

GC05M141953.

H-InvDB

HIX0005267.

HGNC

HGNC:3665. FGF1.

HPA

CAB017519.
HPA003265.

MIM

131220. gene.

PharmGKB

PA28105.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09677.

HOGENOM

HBG715603.

HOVERGEN

P05230.

InParanoid

P05230.

OMA

PSEECLF.

PhylomeDB

P05230.

Enzyme and pathway databases

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.

Reactome

REACT_9470. Signaling by FGFR.

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. IL1_HBGF. 1 hit.

Pfam

PF00167. FGF. 1 hit.
[Graphical view]

PRINTS

PR00263. HBGFFGF.
PR00262. IL1HBGF.

SMART

SM00442. FGF. 1 hit.
[Graphical view]

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00686. Pentosan Polysulfate.

NextBio

9087.

SOURCE

Search...

Entry information

Entry name

FGF1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	February 9, 2010
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.