Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P09038 (FGF2_HUMAN)

Last modified June 16, 2009. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Interacts with CSPG4 and FGFBP1. Found in a complex with FGFBP1, FGF1 and FGF2. Ref.18 Ref.19 Ref.20

Tissue specificity

Expressed in granulosa and cumulus cells.

Post-translational modification

Several N-termini starting at positions 48, 54, 47 and 65 have been identified by direct sequencing.

Miscellaneous

This protein binds heparin more strongly than does aFGF.

Sequence similarities

Belongs to the heparin-binding growth factors family.

Sequence caution

The sequence AAB21432.2 differs from that shown. Reason: Miscellaneous discrepancy. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P09038-1)

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.
Note: Starts at an alternative CUG codon.
Isoform 2 (identifier: P09038-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.
Isoform 3 (identifier: P09038-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.
     15-15: L → M
Note: Starts at an alternative CUG codon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 6464Or 47, or 53, or 46
PRO_0000008932
Chain65 – 210146Heparin-binding growth factor 2
PRO_0000008933

Regions

Region183 – 19917Heparin-binding By similarity
Motif101 – 1033Cell attachment site; atypical Potential
Motif143 – 1453Cell attachment site; atypical Potential

Sites

Binding site911Heparin By similarity

Natural variations

Alternative sequence1 – 5555Missing in isoform 2.
VSP_037383
Alternative sequence1 – 1414Missing in isoform 3.
VSP_037384
Alternative sequence151L → M in isoform 3.
VSP_037385

Secondary structure

............................... 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 26, 2009. Version 2.
Checksum: A21C7A6E82E4F5BD

FASTA21022,623
        10         20         30         40         50         60 
MGDRGRGRAL PGGRLGGRGR GRAPERVGGR GRGRGTAAPR AAPAARGSRP GPAGTMAAGS 

        70         80         90        100        110        120 
ITTLPALPED GGSGAFPPGH FKDPKRLYCK NGGFFLRIHP DGRVDGVREK SDPHIKLQLQ 

       130        140        150        160        170        180 
AEERGVVSIK GVCANRYLAM KEDGRLLASK CVTDECFFFE RLESNNYNTY RSRKYTSWYV 

       190        200        210 
ALKRTGQYKL GSKTGPGQKA ILFLPMSAKS 

« Hide

Isoform 2.

Checksum: BE6CE13373007129
Show »

FASTA15517,254
Isoform 3.

Checksum: D6B5447137E60343
Show »

FASTA19621,203

References

« Hide 'large scale' 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] (ISOFORM 2).
[3]"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] (ISOFORM 2).
[4]"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] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 48-67, ALTERNATIVE INITIATION.
Tissue: Hepatoma.
[5]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed: 19054851] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]NIEHS SNPs program
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]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. expand/collapse author list , 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].
[8]"Basic fibroblast growth factor gene expression."
Florkiewicz R.Z., Shibata F., Barankiewicz T., Baird A., Gonzalez A.M., Florkiewicz E., Shah N.
Ann. N. Y. Acad. Sci. 638:109-126(1991) [PubMed: 1785797] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
[9]"Mutations in the 5' untranslated region of the FGF-2 gene."
Handschug K., Archoukieh E., Glaeser C.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
Tissue: Blood.
[10]"Human amniotic tumor that induces new bone formation in vivo produces growth-regulatory activity in vitro for osteoblasts identified as an extended form of basic fibroblast growth factor."
Izbicka E., Dunstan C., Esparza J., Jacobs C., Sabatini M., Mundy G.R.
Cancer Res. 56:633-636(1996) [PubMed: 8564983] [Abstract]
Cited for: PROTEIN SEQUENCE OF 47-62 (ISOFORMS 1/3).
[11]"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] OF 54-210 (ISOFORMS 1/3), PROTEIN SEQUENCE OF 54-70; 75-82; 87-169; 174-183 AND 189-210 (ISOFORMS 1/3).
Tissue: Hepatoma and Placenta.
[12]"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 57-77.
[13]"Reverse transcription with nested polymerase chain reaction shows expression of basic fibroblast growth factor transcripts in human granulosa and cumulus cells from in vitro fertilisation patients."
Watson R., Anthony F., Pickett M., Lambden P., Masson G.M., Thomas E.J.
Biochem. Biophys. Res. Commun. 187:1227-1231(1992) [PubMed: 1417798] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-182 (ISOFORMS 1/2/3), TISSUE SPECIFICITY.
[14]Zhang H.J., Zhang S.M., Zhuang H.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-210 (ISOFORMS 1/2/3).
[15]"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 65-94.
[16]"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 65-90.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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).
[22]"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).
[23]"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).
[24]"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).
[25]"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).
[26]"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 79-210 IN COMPLEX WITH FGFR2.
[27]"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.

Web resources

Cross-references

Sequence databases

X04431 Genomic DNA. Translation: CAA28027.1.
X04432 Genomic DNA. Translation: CAA28028.1.
X04433 Genomic DNA. Translation: CAA28029.1.
M27968 mRNA. Translation: AAA52448.1.
J04513 mRNA. Translation: AAA52531.1.
J04513 mRNA. Translation: AAA52532.1.
J04513 mRNA. Translation: AAA52533.1.
AB451321 mRNA. Translation: BAG70135.1.
AB451450 mRNA. Translation: BAG70264.1.
EF506888 Genomic DNA. Translation: ABO43041.1.
CH471056 Genomic DNA. Translation: EAX05222.1.
S81809 Genomic DNA. Translation: AAB21432.2. Sequence problems.
Y13468 Genomic DNA. Translation: CAA73868.1.
M17599 mRNA. Translation: AAA52534.1.
AY820133 mRNA. Translation: AAV70487.1.
S47380 mRNA. Translation: AAD13853.1.
IPIIPI00154603.
PIRA32398.
RefSeqNP_001997.5.
UniGeneHs.284244

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BASX-ray1.90A57-210[»]
1BFBX-ray1.90A64-210[»]
1BFCX-ray2.20A64-210[»]
1BFFX-ray2.00A82-210[»]
1BFGX-ray1.60A65-210[»]
1BLANMR-A56-210[»]
1BLDNMR-A56-210[»]
1CVSX-ray2.80A/B79-210[»]
1EV2X-ray2.20A/B/C/D79-210[»]
1FGAX-ray2.20A65-210[»]
1FQ9X-ray3.00A/B79-210[»]
1II4X-ray2.70A/B/C/D56-210[»]
1IILX-ray2.30A/B/C/D56-210[»]
2BFHX-ray2.50A83-210[»]
2FGFX-ray1.77A65-210[»]
4FGFX-ray1.60A65-210[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4012N.
IntActP09038. 5 interactions.

Proteomic databases

PRIDEP09038.

Genome annotation databases

EnsemblENSG00000138685. Homo sapiens. [Contig view]
GeneID2247.
KEGGhsa:2247.

Organism-specific databases

GeneCardsGC04P124027.
H-InvDBHIX0031422.
HGNCHGNC:3676. FGF2.
HPACAB000125.
MIM134920. gene.
PharmGKBPA28115.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP09038.

Enzyme and pathway databases

Pathway_Interaction_DBangiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
fgf_pathway. FGF signaling pathway.
glypican_1pathway. Glypican 1 network.
avb3_integrin_pathway. Integrins in angiogenesis.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
ReactomeREACT_9470. Signaling by FGFR.

Gene expression databases

ArrayExpressP09038.
BgeeP09038.
CleanExHS_FGF2.
GermOnlineENSG00000138685. Homo sapiens.

Family and domain databases

ProDomPD000831. IL1_HBGF. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00686. Pentosan Polysulfate.
NextBio9095.
SOURCESearch...

Entry information

Entry nameFGF2_HUMAN
AccessionPrimary (citable) accession number: P09038
Secondary accession number(s): A4LBB8 expand/collapse secondary AC list , O00527, P78443, Q16443, Q5PY50, Q7KZ11, Q7KZ72, Q9UC54
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: May 26, 2009
Last modified: June 16, 2009
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents