Heparin-binding growth factor 2 precursor

Clusters with 100%, 90%, 50% identity |

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Names and origin

Protein names

Recommended name:
    Heparin-binding growth factor 2
      Short name=HBGF-2
Alternative name(s):
    Basic fibroblast growth factor
      Short name=BFGF

Gene names

Name:	FGF2
Synonyms:	FGFB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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. Interacts with CSPG4 and FGFBP1. Found in a complex with FGFBP1, FGF1 and FGF2.
Miscellaneous	This protein binds heparin more strongly than does aFGF.
Sequence similarities	Belongs to the heparin-binding growth factors family.

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Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	Ras protein signal transduction Traceable author statement. Source: ProtInc activation of MAPK activity Traceable author statement. Source: ProtInc chemotaxis Traceable author statement. Source: ProtInc fibroblast growth factor receptor signaling pathway Inferred from Experiment. Source: Reactome nervous system development Traceable author statement. Source: ProtInc organ morphogenesis Traceable author statement. Source: ProtInc positive regulation of cardiac muscle cell proliferation Inferred from direct assay. Source: UniProtKB
Cellular component	extracellular space Ref.4 Traceable author statement. Source: ProtInc
Molecular function	protein binding Ref.12 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CASP1	P29466	1	EBI-977447,EBI-516667
FGFBP1	Q14512	3	EBI-977447,EBI-953742
FGFR2	P21802-5	1	EBI-977447,EBI-1028732

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Propeptide

1 – 9

Chain

10 – 155

146

Heparin-binding growth factor 2

Regions

Region

128 – 144

Heparin-binding By similarity

Motif

46 – 48

Cell attachment site; atypical Potential

Motif

88 – 90

Cell attachment site; atypical Potential

Sites

Binding site

Heparin By similarity

Secondary structure

155

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P09038-1 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: BE6CE13373007129
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FASTA

155

17,254

        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

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References

[1]	"Human basic fibroblast growth factor: nucleotide sequence, genomic organization, and expression in mammalian cells." Abraham J.A., Whang J.L., Tumolo A., Mergia A., Fiddes J.C. Cold Spring Harb. Symp. Quant. Biol. 51:657-668(1986) [PubMed: 3472745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Human basic fibroblast growth factor: nucleotide sequence and genomic organization." Abraham J.A., Whang J.L., Tumolo A., Mergia A., Friedman J., Gospodarowicz D., Fiddes J.C. EMBO J. 5:2523-2528(1986) [PubMed: 3780670] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"A form of human basic fibroblast growth factor with an extended amino terminus." Sommer A., Brewer M.T., Thompson R.C., Moscatelli D., Presta M., Rifkin D.B. Biochem. Biophys. Res. Commun. 144:543-550(1987) [PubMed: 3579930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning and expression of cDNA encoding human basic fibroblast growth factor." Kurokawa T., Sasada R., Iwane M., Igarashi K. FEBS Lett. 213:189-194(1987) [PubMed: 2435575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"High molecular mass forms of basic fibroblast growth factor are initiated by alternative CUG codons." 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. Proc. Natl. Acad. Sci. U.S.A. 86:1836-1840(1989) [PubMed: 2538817] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"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 10-35.
[7]	"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 10-39.
[8]	"Amino-terminal sequence of a large form of basic fibroblast growth factor isolated from human benign prostatic hyperplastic tissue." Story M.T., Esch F., Shimasaki S., Sasse J., Jacobs S.C., Lawson R.K. Biochem. Biophys. Res. Commun. 142:702-709(1987) [PubMed: 2435284] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22.
[9]	"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 FGF1.
[10]	"High-affinity binding of basic fibroblast growth factor and platelet-derived growth factor-AA to the core protein of the NG2 proteoglycan." Goretzki L., Burg M.A., Grako K.A., Stallcup W.B. J. Biol. Chem. 274:16831-16837(1999) [PubMed: 10358027] [Abstract] Cited for: INTERACTION WITH CSPG4.
[11]	"Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein." Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A., Wellstein A. J. Biol. Chem. 276:40247-40253(2001) [PubMed: 11509569] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[12]	"Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display." Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y., Tomita Y., Riegel A.T., Wellstein A. J. Biol. Chem. 281:1137-1144(2006) [PubMed: 16257968] [Abstract] Cited for: INTERACTION WITH FGFBP1.
[13]	"Crystal structure of basic fibroblast growth factor at 1.6-A resolution." Ago H., Kitagawa Y., Fujishima A., Matsuura Y., Katsube Y. J. Biochem. 110:360-363(1991) [PubMed: 1769963] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[14]	"Three-dimensional structure of human basic fibroblast growth factor." Eriksson A.E., Cousens L.S., Weaver L.H., Matthews B.W. Proc. Natl. Acad. Sci. U.S.A. 88:3441-3445(1991) [PubMed: 1707542] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[15]	"Three-dimensional structure of human basic fibroblast growth factor, a structural homolog of interleukin 1 beta." Zhang J., Cousens L.S., Barr P.J., Sprang S.R. Proc. Natl. Acad. Sci. U.S.A. 88:3446-3450(1991) [PubMed: 1849658] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[16]	"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 (2.8 ANGSTROMS).
[17]	"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." Eriksson A.E., Cousens L.S., Matthews B.W. Protein Sci. 2:1274-1284(1993) [PubMed: 7691311] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[18]	"Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome." Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M. Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001) [PubMed: 11390973] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-155 IN COMPLEX WITH FGFR2.
[19]	"High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy." Moy F.J., Seddon A.P., Boehlen P., Powers R. Biochemistry 35:13552-13561(1996) [PubMed: 8885834] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X04431 Genomic DNA. Translation: CAA28027.1.
X04432 Genomic DNA. Translation: CAA28028.1.
X04433 Genomic DNA. Translation: CAA28029.1.
M17599 mRNA. Translation: AAA52534.1. Different initiation.
M27968 mRNA. Translation: AAA52448.1.
J04513 mRNA. Translation: AAA52533.1. Different initiation.

PIR

A32398.

RefSeq

NP_001997.5.

UniGene

Hs.284244

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BAS	X-ray	1.90	A	2-155	[»]
1BFB	X-ray	1.90	A	9-155	[»]
1BFC	X-ray	2.20	A	9-155	[»]
1BFF	X-ray	2.00	A	27-155	[»]
1BFG	X-ray	1.60	A	10-155	[»]
1BLA	NMR	-	A	1-155	[»]
1BLD	NMR	-	A	1-155	[»]
1CVS	X-ray	2.80	A/B	24-155	[»]
1EV2	X-ray	2.20	A/B/C/D	24-155	[»]
1FGA	X-ray	2.20	A	10-155	[»]
1FQ9	X-ray	3.00	A/B	24-155	[»]
1II4	X-ray	2.70	A/B/C/D	1-155	[»]
1IIL	X-ray	2.30	A/B/C/D	1-155	[»]
2BFH	X-ray	2.50	A	28-155	[»]
2FGF	X-ray	1.77	A	10-155	[»]
4FGF	X-ray	1.60	A	10-155	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:4012N.

IntAct

P09038.

Genome annotation databases

Ensembl

ENSG00000138685. Homo sapiens. [Contig view]

GeneID

2247.

KEGG

hsa:2247.

Organism-specific databases

H-InvDB

HIX0031422.

HGNC

HGNC:3676. FGF2.

HPA

CAB000125.

MIM

134920. gene.

PharmGKB

PA28115.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

P09038.

Enzyme and pathway databases

Reactome

REACT_9470. Signaling by FGFR.

Gene expression databases

ArrayExpress

P09038.

CleanEx

HS_FGF2.

GermOnline

ENSG00000138685. Homo sapiens.

Family and domain databases

InterPro

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.

ProDom

PD000831. IL1_HBGF. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00442. FGF. 1 hit.
[Graphical view]

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

BLOCKS

Search...

Other Resources

DrugBank

DB00686. Pentosan Polysulfate.

LinkHub

P09038.

SOURCE

Search...

ProtoNet

Search...

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Entry information

Entry name

FGF2_HUMAN

Accession

Primary (citable) accession number: P09038

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	September 2, 2008
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents