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UniProtKB/Swiss-Prot entry P09038


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FGF2_HUMAN
Primary accession number P09038
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on November 1, 1988 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 119)
Name and origin of the protein
Protein name Heparin-binding growth factor 2 [Precursor]
Synonyms HBGF-2
Basic fibroblast growth factor
BFGF
Gene name
Name: FGF2
Synonyms: FGFB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[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
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]
PIR A32398; A32398.
RefSeq NP_001997.5; -.
UniGene Hs.284244
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; 5.
Enzyme and pathway databases
Reactome REACT_9470; Signaling by FGFR.
Organism-specific databases
GeneCards GC04P124027; -.
H-InvDB HIX0031422; -.
HGNC HGNC:3676; FGF2.
GenAtlas FGF2.
HPA CAB000125; -.
MIM 134920; gene. [NCBI / EBI]
PharmGKB PA28115; -.
GeneCards P09038.
Gene expression databases
ArrayExpress P09038; -.
CleanEx HS_FGF2; -.
GermOnline ENSG00000138685; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0008083; Molecular function: growth factor activity (inferred from electronic annotation from InterPro).
GO:0008201; Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
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:0043537; Biological process: negative regulation of blood vessel endothelial cell migration (inferred from direct assay from UniProtKB).
GO:0043536; Biological process: positive regulation of blood vessel endothelial cell migration (inferred from direct assay from UniProtKB).
GO:0060045; Biological process: positive regulation of cardiac muscle cell proliferation (inferred from direct assay from UniProtKB).
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
SWISS-3DIMAGE P09038.
Proteomics databases
PRIDE P09038; -.
Genome annotation databases
Ensembl ENSG00000138685; Homo sapiens. [Contig view]
GeneID 2247; -.
KEGG hsa:2247; -.
Phylogenomic databases
HOVERGEN P09038; -.
Other
DrugBank DB00686; Pentosan Polysulfate.
LinkHub P09038; -.
NextBio 9095; -.
SOURCE FGF2; Homo sapiens.
ProtoNet P09038.
UniRef 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
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   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   3     6  4      
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

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