[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3472745 [NCBI, ExPASy, EBI, Israel, Japan] Abraham J.A., Whang J.L., Tumolo A., Mergia A., Fiddes J.C.; "Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells."; Cold Spring Harb. Symp. Quant. Biol. 51:657-668(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. PubMed=3780670 [NCBI, ExPASy, EBI, Israel, Japan] Abraham J.A., Whang J.L., Tumolo A., Mergia A., Friedman J., Gospodarowicz D., Fiddes J.C.; "Human basic fibroblast growth factor: nucleotide sequence and genomic organization."; EMBO J. 5:2523-2528(1986).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/S0006-291X(87)80001-3; PubMed=3579930 [NCBI, ExPASy, EBI, Israel, Japan] Sommer A., Brewer M.T., Thompson R.C., Moscatelli D., Presta M., Rifkin D.B.; "A form of human basic fibroblast growth factor with an extended amino terminus."; Biochem. Biophys. Res. Commun. 144:543-550(1987).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-5793(87)81489-8; PubMed=2435575 [NCBI, ExPASy, EBI, Israel, Japan] Kurokawa T., Sasada R., Iwane M., Igarashi K.; "Cloning and expression of cDNA encoding human basic fibroblast growth factor."; FEBS Lett. 213:189-194(1987).
[5]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2538817 [NCBI, ExPASy, EBI, Israel, Japan] Prats H., Kaghad M., Prats A.C., Klagsbrun M., Lelias J.M., Liauzun P., Chalon P., Tauber J.P., Amalric F., Smith J.A., Caput D.; "High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons."; Proc. Natl. Acad. Sci. U.S.A. 86:1836-1840(1989).
[6]	PROTEIN SEQUENCE OF 10-35. DOI=10.1016/0014-5793(86)80812-2; PubMed=3732516 [NCBI, ExPASy, EBI, Israel, Japan] Gautschi P., Frater-Schroeder M., Boehlen P.; "Partial molecular characterization of endothelial cell mitogens from human brain: acidic and basic fibroblast growth factors."; FEBS Lett. 204:203-207(1986).
[7]	PROTEIN SEQUENCE OF 10-39. DOI=10.1016/0006-291X(86)90028-8; PubMed=3964259 [NCBI, ExPASy, EBI, Israel, Japan] Gimenez-Gallego G., Conn G., Hatcher V.B., Thomas K.A.; "Human brain-derived acidic and basic fibroblast growth factors: amino terminal sequences and specific mitogenic activities."; Biochem. Biophys. Res. Commun. 135:541-548(1986).
[8]	PROTEIN SEQUENCE OF 2-22. DOI=10.1016/0006-291X(87)91471-9; PubMed=2435284 [NCBI, ExPASy, EBI, Israel, Japan] Story M.T., Esch F., Shimasaki S., Sasse J., Jacobs S.C., Lawson R.K.; "Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue."; Biochem. Biophys. Res. Commun. 142:702-709(1987).
[9]	IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF1. PubMed=1885605 [NCBI, ExPASy, EBI, Israel, Japan] Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.; "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors."; J. Biol. Chem. 266:16778-16785(1991).
[10]	INTERACTION WITH CSPG4. DOI=10.1074/jbc.274.24.16831; PubMed=10358027 [NCBI, ExPASy, EBI, Israel, Japan] Goretzki L., Burg M.A., Grako K.A., Stallcup W.B.; "High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan."; J. Biol. Chem. 274:16831-16837(1999).
[11]	INTERACTION WITH FGFBP1. DOI=10.1074/jbc.M104933200; PubMed=11509569 [NCBI, ExPASy, EBI, Israel, Japan] Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A., Wellstein A.; "Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein."; J. Biol. Chem. 276:40247-40253(2001).
[12]	INTERACTION WITH FGFBP1. DOI=10.1074/jbc.M510754200; PubMed=16257968 [NCBI, ExPASy, EBI, Israel, Japan] Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y., Tomita Y., Riegel A.T., Wellstein A.; "Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display."; J. Biol. Chem. 281:1137-1144(2006).
[13]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). PubMed=1769963 [NCBI, ExPASy, EBI, Israel, Japan] Ago H., Kitagawa Y., Fujishima A., Matsuura Y., Katsube Y.; "Crystal structure of basic fibroblast growth factor at 1.6-A resolution."; J. Biochem. 110:360-363(1991).
[14]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). PubMed=1707542 [NCBI, ExPASy, EBI, Israel, Japan] Eriksson A.E., Cousens L.S., Weaver L.H., Matthews B.W.; "Three-dimensional structure of human basic fibroblast growth factor."; Proc. Natl. Acad. Sci. U.S.A. 88:3441-3445(1991).
[15]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). PubMed=1849658 [NCBI, ExPASy, EBI, Israel, Japan] Zhang J., Cousens L.S., Barr P.J., Sprang S.R.; "Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta."; Proc. Natl. Acad. Sci. U.S.A. 88:3446-3450(1991).
[16]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). PubMed=1702556 [NCBI, ExPASy, EBI, Israel, Japan] Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C.; "Three-dimensional structures of acidic and basic fibroblast growth factors."; Science 251:90-93(1991).
[17]	X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). PubMed=7691311 [NCBI, ExPASy, EBI, Israel, Japan] Eriksson A.E., Cousens L.S., Matthews B.W.; "Refinement of the structure of human basic fibroblast growth factor at 1.6-A resolution and analysis of presumed heparin binding sites by selenate substitution."; Protein Sci. 2:1274-1284(1993).
[18]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-155 IN COMPLEX WITH FGFR2. DOI=10.1073/pnas.121183798; PubMed=11390973 [NCBI, ExPASy, EBI, Israel, Japan] Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M.; "Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome."; Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001).
[19]	STRUCTURE BY NMR. DOI=10.1021/bi961260p; PubMed=8885834 [NCBI, ExPASy, EBI, Israel, Japan] Moy F.J., Seddon A.P., Boehlen P., Powers R.; "High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy."; Biochemistry 35:13552-13561(1996).

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: Monomer. Interacts with CSPG4 and FGFBP1. Found in a complex with FGFBP1, FGF1 and FGF2.
INTERACTION:
P29466:CASP1; NbExp=1; IntAct=EBI-977447, EBI-516667;
Q14512:FGFBP1; NbExp=3; IntAct=EBI-977447, EBI-953742;
P21802-5:FGFR2; NbExp=1; IntAct=EBI-977447, EBI-1028732;
MISCELLANEOUS: This protein binds heparin more strongly than does aFGF.
SIMILARITY: Belongs to the heparin-binding growth factors family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X04431; CAA28027.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04432; CAA28028.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04433; CAA28029.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17599; AAA52534.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27968; AAA52448.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J04513; AAA52533.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A32398; A32398.

NP_001997.5; -.

3D structure databases

PDB

1BAS; X-ray; 1.90 A; A=2-155.	[ExPASy / RCSB / EBI]
1BFB; X-ray; 1.90 A; A=9-155.	[ExPASy / RCSB / EBI]
1BFC; X-ray; 2.20 A; A=9-155.	[ExPASy / RCSB / EBI]
1BFF; X-ray; 2.00 A; A=27-155.	[ExPASy / RCSB / EBI]
1BFG; X-ray; 1.60 A; A=10-155.	[ExPASy / RCSB / EBI]
1BLA; NMR; -; A=1-155.	[ExPASy / RCSB / EBI]
1BLD; NMR; -; A=1-155.	[ExPASy / RCSB / EBI]
1CVS; X-ray; 2.80 A; A/B=24-155.	[ExPASy / RCSB / EBI]
1EV2; X-ray; 2.20 A; A/B/C/D=24-155.	[ExPASy / RCSB / EBI]
1FGA; X-ray; 2.20 A; A=10-155.	[ExPASy / RCSB / EBI]
1FQ9; X-ray; 3.00 A; A/B=24-155.	[ExPASy / RCSB / EBI]
1II4; X-ray; 2.70 A; A/B/C/D=1-155.	[ExPASy / RCSB / EBI]
1IIL; X-ray; 2.30 A; A/B/C/D=1-155.	[ExPASy / RCSB / EBI]
2BFH; X-ray; 2.50 A; A=28-155.	[ExPASy / RCSB / EBI]
2FGF; X-ray; 1.77 A; A=10-155.	[ExPASy / RCSB / EBI]
4FGF; X-ray; 1.60 A; A=10-155.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BAS; -.
1BFB; -.
1BFC; -.
1BFF; -.
1BFG; -.
1BLA; -.
1BLD; -.
1CVS; -.
1EV2; -.
1FGA; -.
1FQ9; -.
1II4; -.
1IIL; -.
2BFH; -.
2FGF; -.
4FGF; -.

ModBase

P09038.

Protein-protein interaction databases

DIP

DIP:4012N; -.

IntAct

P09038; -.

Enzyme and pathway databases

Reactome

REACT_9470; Signaling by FGFR.

Organism-specific databases

HIX0031422; -.

HGNC:3676; FGF2.

FGF2; Homo sapiens.

CAB000125; -.

134920; gene. [NCBI / EBI]

PharmGKB

PA28115; -.

GeneCards

P09038.

Gene expression databases

ArrayExpress

P09038; -.

CleanEx

HS_FGF2; -.

GermOnline

ENSG00000138685; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0000187;	Biological process: activation of MAPK activity (traceable author statement from ProtInc).
GO:0006935;	Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0008543;	Biological process: fibroblast growth factor receptor signaling pathway (inferred from experiment from Reactome).
GO:0007399;	Biological process: nervous system development (traceable author statement from ProtInc).
GO:0009887;	Biological process: organ morphogenesis (traceable author statement from ProtInc).
GO:0008284;	Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
GO:0007265;	Biological process: Ras protein signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002209; GF_heparin_bd.
IPR002348; IL1_HBGF.
Graphical view of domain structure.

PANTHER

PTHR11486; IL1_HBGF; 1.

Pfam

PF00167; FGF; 1.
Pfam graphical view of domain structure.

PRINTS

PR00263; HBGFFGF.
PR00262; IL1HBGF.

ProDom

PD000831; IL1_HBGF; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00442; FGF; 1.
SMART graphical view of domain structure.

PROSITE

PS00247; HBGF_FGF; 1.

Other

Genome annotation databases

Ensembl

ENSG00000138685; Homo sapiens. [Contig view]

GeneID

2247; -.

KEGG

hsa:2247; -.

Phylogenomic databases

HOVERGEN

P09038; -.

Other

DrugBank

DB00686; Pentosan Polysulfate.

P09038; -.

FGF2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Angiogenesis; Developmental protein; Differentiation; Direct protein sequencing; Growth factor; Heparin-binding; Mitogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 9`	`9`		`PRO_0000008932`
`CHAIN`	`10 155`	`146`	`Heparin-binding growth factor 2.`	`PRO_0000008933`
`REGION`	`128 144`	`17`	`Heparin-binding (By similarity).`
`MOTIF`	`46 48`	`3`	`Cell attachment site; atypical (Potential).`
`MOTIF`	`88 90`	`3`	`Cell attachment site; atypical (Potential).`
`BINDING`	`36 36`		`Heparin (By similarity).`
`STRAND`	`30 34`	`5`
`TURN`	`35 38`	`4`
`STRAND`	`39 43`	`5`
`STRAND`	`49 52`	`4`
`HELIX`	`58 60`	`3`
`STRAND`	`62 68`	`7`
`STRAND`	`71 76`	`6`
`TURN`	`77 80`	`4`
`STRAND`	`81 85`	`5`
`STRAND`	`91 96`	`6`
`HELIX`	`99 101`	`3`
`STRAND`	`103 107`	`5`
`STRAND`	`113 120`	`8`
`STRAND`	`131 133`	`3`
`HELIX`	`136 138`	`3`
`HELIX`	`144 146`	`3`
`STRAND`	`148 151`	`4`

Sequence information

Length: 155 AA [This is the length of the unprocessed precursor]

Molecular weight: 17254 Da [This is the MW of the unprocessed precursor]

CRC64: BE6CE13373007129 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAGSITTLP ALPEDGGSGA FPPGHFKDPK RLYCKNGGFF LRIHPDGRVD GVREKSDPHI 

        70         80         90        100        110        120 
KLQLQAEERG VVSIKGVCAN RYLAMKEDGR LLASKCVTDE CFFFERLESN NYNTYRSRKY 

       130        140        150 
TSWYVALKRT GQYKLGSKTG PGQKAILFLP MSAKS

P09038 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools