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P09038 (FGF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor 2

Short name=FGF-2
Alternative name(s):
Basic fibroblast growth factor
Short name=bFGF
Heparin-binding growth factor 2
Short name=HBGF-2
Gene names
Name:FGF2
Synonyms:FGFB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. Ref.11 Ref.20

Subunit structure

Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Interacts with CSPG4, FGFBP1 and TEC. Found in a complex with FGFBP1, FGF1 and FGF2. Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Subcellular location

Secreted. Nucleus. Note: Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane. Binding of exogenous FGF2 to FGFR facilitates endocytosis followed by translocation of FGF2 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as CEP57. Ref.25 Ref.28

Tissue specificity

Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non-cancerous liver tissue. Ref.11 Ref.18

Post-translational modification

Phosphorylation at Tyr-215 regulates FGF2 unconventional secretion.

Several N-termini starting at positions 94, 125, 126, 132, 143 and 162 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.

Biophysicochemical properties

pH dependence:

Retains almost half of its activity after treatment at pH 2.0 for 3 hours at 20 degrees Celsius. Ref.11

Temperature dependence:

Inactivated after 3 minutes at 60 degrees Celsius or 1 minute at 80 degrees Celsius.

Sequence caution

The sequence AAA52448.1 differs from that shown. Reason: Frameshift at positions 25, 82, 98 and 133.

The sequence AAB21432.2 differs from that shown. Reason: Frameshift at position 25.

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

The sequence ABO43041.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence ABO43041.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence CAA28027.1 differs from that shown. Reason: Frameshift at positions 25 and 102.

The sequence CAA28027.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence CAA73868.1 differs from that shown. Reason: Frameshift at position 25.

The sequence CAA73868.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence EAX05222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence EAX05222.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentNucleus
Secreted
   Coding sequence diversityAlternative initiation
   LigandHeparin-binding
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processC21-steroid hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MAPK import into nucleus

Inferred from electronic annotation. Source: Ensembl

Ras protein signal transduction

Traceable author statement PubMed 10848592. Source: ProtInc

activation of MAPK activity

Traceable author statement PubMed 9712850. Source: ProtInc

activation of MAPKK activity

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from direct assay PubMed 12631064. Source: UniProtKB

cell migration involved in sprouting angiogenesis

Inferred from direct assay PubMed 18059339. Source: BHF-UCL

chemotaxis

Traceable author statement PubMed 10848592. Source: ProtInc

chondroblast differentiation

Inferred from direct assay PubMed 17167778. Source: UniProtKB

corticotropin hormone secreting cell differentiation

Inferred from electronic annotation. Source: Ensembl

embryonic morphogenesis

Traceable author statement PubMed 20011604. Source: DFLAT

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Inferred from direct assay PubMed 17500071. Source: UniProtKB

glial cell differentiation

Inferred from electronic annotation. Source: Ensembl

hyaluronan catabolic process

Inferred from direct assay PubMed 19577615. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

inositol phosphate biosynthetic process

Inferred from direct assay PubMed 20011604. Source: DFLAT

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lung development

Inferred from electronic annotation. Source: Ensembl

mammary gland epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

negative regulation of cell death

Inferred from direct assay PubMed 12631064. Source: UniProtKB

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of fibroblast migration

Inferred from direct assay PubMed 19577615. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

negative regulation of wound healing

Inferred from direct assay PubMed 19577615. Source: UniProtKB

nervous system development

Traceable author statement PubMed 9576942. Source: ProtInc

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

organ induction

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Traceable author statement PubMed 10903182. Source: ProtInc

phosphatidylinositol biosynthetic process

Inferred from direct assay PubMed 20011604. Source: DFLAT

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive chemotaxis

Inferred from direct assay PubMed 18059339. Source: GOC

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 17167778. Source: UniProtKB

positive regulation of angiogenesis

Inferred from direct assay PubMed 20011604. Source: DFLAT

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

positive regulation of cardiac muscle cell proliferation

Inferred from direct assay PubMed 9553078. Source: BHF-UCL

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell fate specification

Inferred from direct assay PubMed 18635606. Source: MGI

positive regulation of cell proliferation

Inferred from genetic interaction Ref.20. Source: MGI

positive regulation of cerebellar granule cell precursor proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 18059339. Source: BHF-UCL

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from direct assay PubMed 20011604. Source: DFLAT

positive regulation of phospholipase C activity

Inferred from direct assay PubMed 20011604. Source: DFLAT

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18059339. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17500071. Source: UniProtKB

regulation of angiogenesis

Traceable author statement PubMed 20011604. Source: DFLAT

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of retinal cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 20011604. Source: DFLAT

response to axon injury

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement PubMed 9712850. Source: ProtInc

stem cell development

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from electronic annotation. Source: Ensembl

thyroid-stimulating hormone-secreting cell differentiation

Inferred from electronic annotation. Source: Ensembl

wound healing

Traceable author statement PubMed 20011604. Source: DFLAT

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement Ref.10. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchemoattractant activity

Inferred from direct assay PubMed 18059339. Source: BHF-UCL

cytokine activity

Inferred from direct assay PubMed 18059339. Source: BHF-UCL

fibroblast growth factor receptor binding

Inferred from physical interaction PubMed 10830168. Source: MGI

growth factor activity

Inferred from direct assay PubMed 18059339. Source: BHF-UCL

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay PubMed 17500071. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative initiation. [Align] [Select]
Isoform 1 (identifier: P09038-4)

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: P09038-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
     79-79: L → M
Note: Starts at an alternative CUG codon.
Isoform 3 (identifier: P09038-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
Isoform 4 (identifier: P09038-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.
     93-93: L → M
Note: Starts at an alternative CUG codon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 142142Or 93, or 124, or 125, or 131, or 161
PRO_0000008932
Chain143 – 288146Fibroblast growth factor 2
PRO_0000008933

Regions

Region261 – 27717Heparin-binding By similarity
Motif179 – 1813Cell attachment site; atypical Potential
Motif221 – 2233Cell attachment site; atypical Potential

Sites

Binding site1691Heparin By similarity

Amino acid modifications

Modified residue1081Omega-N-methylarginine; alternate By similarity
Modified residue1081Symmetric dimethylarginine; alternate By similarity
Modified residue1101Omega-N-methylarginine; alternate By similarity
Modified residue1101Symmetric dimethylarginine; alternate By similarity
Modified residue1121Omega-N-methylarginine; alternate By similarity
Modified residue1121Symmetric dimethylarginine; alternate By similarity
Modified residue2151Phosphotyrosine; by TEC Ref.25

Natural variations

Alternative sequence1 – 133133Missing in isoform 3.
VSP_037383
Alternative sequence1 – 9292Missing in isoform 4.
VSP_037384
Alternative sequence1 – 7878Missing in isoform 2.
VSP_038236
Alternative sequence791L → M in isoform 2.
VSP_038237
Alternative sequence931L → M in isoform 4.
VSP_037385

Experimental info

Sequence conflict251G → R in AAA52448. Ref.10
Sequence conflict501H → Q in AAA52448. Ref.10
Sequence conflict591A → R in AAA52448. Ref.10

Secondary structure

.......................................... 288
Helix Strand Turn

Details...

Sequences

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

Last modified October 13, 2009. Version 3.
Checksum: EAE98552A39D5E19

FASTA28830,770
        10         20         30         40         50         60 
MVGVGGGDVE DVTPRPGGCQ ISGRGARGCN GIPGAAAWEA ALPRRRPRRH PSVNPRSRAA 

        70         80         90        100        110        120 
GSPRTRGRRT EERPSGSRLG DRGRGRALPG GRLGGRGRGR APERVGGRGR GRGTAAPRAA 

       130        140        150        160        170        180 
PAARGSRPGP AGTMAAGSIT TLPALPEDGG SGAFPPGHFK DPKRLYCKNG GFFLRIHPDG 

       190        200        210        220        230        240 
RVDGVREKSD PHIKLQLQAE ERGVVSIKGV CANRYLAMKE DGRLLASKCV TDECFFFERL 

       250        260        270        280 
ESNNYNTYRS RKYTSWYVAL KRTGQYKLGS KTGPGQKAIL FLPMSAKS 

« Hide

Isoform 2 [UniParc].

Checksum: A21C7A6E82E4F5BD
Show »

FASTA21022,623
Isoform 3 [UniParc].

Checksum: BE6CE13373007129
Show »

FASTA15517,254
Isoform 4 [UniParc].

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), PROTEIN SEQUENCE OF 126-145 (ISOFORMS 1/2/4), ALTERNATIVE INITIATION.
Tissue: Hepatoma.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]NIEHS SNPs program
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
[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 1-192.
Tissue: Blood.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-288 (ISOFORM 1).
[11]"Characterization of high-molecular-mass forms of basic fibroblast growth factor produced by hepatocellular carcinoma cells: possible involvement of basic fibroblast growth factor in hepatocarcinogenesis."
Shimoyama Y., Gotoh M., Ino Y., Sakamoto M., Kato K., Hirohashi S.
Jpn. J. Cancer Res. 82:1263-1270(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 94-107 AND 162-173, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Hepatoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 125-140 (ISOFORMS 1/2/4).
[13]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 132-288 (ISOFORMS 1/2/4), PROTEIN SEQUENCE OF 132-148; 153-160; 165-247; 252-261 AND 267-288 (ISOFORMS 2/4).
Tissue: Hepatoma and Placenta.
[14]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 135-155 (ISOFORMS 1/2/3/4).
[15]Zhang H.J., Zhang S.M., Zhuang H.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 143-288 (ISOFORMS 1/2/3/4).
[16]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 143-172 (ISOFORMS 1/2/3/4).
[17]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 143-168 (ISOFORMS 1/2/3/4).
[18]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 173-260 (ISOFORMS 1/2/3/4), TISSUE SPECIFICITY.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH FGFBP1 AND FGF1.
[20]"Receptor specificity of the fibroblast growth factor family."
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., Gao G., Goldfarb M.
J. Biol. Chem. 271:15292-15297(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, FUNCTION IN CELL PROLIFERATION.
[21]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSPG4.
[22]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFBP1.
[23]"Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor."
Skjerpen C.S., Wesche J., Olsnes S.
J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF1.
[24]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGFBP1.
[25]"Tec-kinase-mediated phosphorylation of fibroblast growth factor 2 is essential for unconventional secretion."
Ebert A.D., Laussmann M., Wegehingel S., Kaderali L., Erfle H., Reichert J., Lechner J., Beer H.D., Pepperkok R., Nickel W.
Traffic 11:813-826(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-215, INTERACTION WITH TEC, SUBCELLULAR LOCATION.
[26]"Cellular signaling by fibroblast growth factor receptors."
Eswarakumar V.P., Lax I., Schlessinger J.
Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[27]"Fibroblast growth factor signalling: from development to cancer."
Turner N., Grose R.
Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[28]"Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnalpha1 and Kpnbeta1."
Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y., Walchli S., Olsnes S., Wiedlocha A.
Traffic 13:650-664(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[29]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
[30]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 143-288.
[31]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 143-288.
[32]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 135-288.
[33]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 143-288.
[34]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 134-288 IN COMPLEX WITH FGFR2.
[35]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 134-288.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04431 Genomic DNA. Translation: CAA28027.1. Sequence problems.
X04432 Genomic DNA. Translation: CAA28028.1.
X04433 Genomic DNA. Translation: CAA28029.1.
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. Sequence problems.
AC021205 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX05222.1. Sequence problems.
S81809 Genomic DNA. Translation: AAB21432.2. Sequence problems.
Y13468 Genomic DNA. Translation: CAA73868.1. Sequence problems.
M27968 mRNA. Translation: AAA52448.1. Frameshift.
M17599 mRNA. Translation: AAA52534.1.
AY820133 mRNA. Translation: AAV70487.1.
S47380 mRNA. Translation: AAD13853.1.
PIRA32398.
RefSeqNP_001997.5. NM_002006.4.
UniGeneHs.284244.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BASX-ray1.90A135-288[»]
1BFBX-ray1.90A142-288[»]
1BFCX-ray2.20A142-288[»]
1BFFX-ray2.00A160-288[»]
1BFGX-ray1.60A143-288[»]
1BLANMR-A134-288[»]
1BLDNMR-A134-288[»]
1CVSX-ray2.80A/B157-288[»]
1EV2X-ray2.20A/B/C/D157-288[»]
1FGAX-ray2.20A143-288[»]
1FQ9X-ray3.00A/B157-288[»]
1II4X-ray2.70A/B/C/D134-288[»]
1IILX-ray2.30A/B/C/D134-288[»]
2BFHX-ray2.50A161-288[»]
2FGFX-ray1.77A143-288[»]
2M49NMR-A/C161-286[»]
4FGFX-ray1.60A143-288[»]
ProteinModelPortalP09038.
SMRP09038. Positions 134-288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108538. 19 interactions.
DIPDIP-4012N.
IntActP09038. 6 interactions.
MINTMINT-222469.

Chemistry

BindingDBP09038.
ChEMBLCHEMBL3107.
DrugBankDB00686. Pentosan Polysulfate.

PTM databases

PhosphoSiteP09038.

Polymorphism databases

DMDM261260095.

Proteomic databases

PaxDbP09038.
PRIDEP09038.

Protocols and materials databases

DNASU2247.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000608478; ENSP00000477134; ENSG00000138685. [P09038-2]
GeneID2247.
KEGGhsa:2247.
UCSCuc003iev.1. human. [P09038-4]

Organism-specific databases

CTD2247.
GeneCardsGC04P123747.
HGNCHGNC:3676. FGF2.
HPACAB000125.
MIM134920. gene.
neXtProtNX_P09038.
PharmGKBPA28115.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325757.
HOVERGENHBG107917.
InParanoidP09038.
KOK04358.
OrthoDBEOG7992S1.
PhylomeDBP09038.
TreeFamTF317805.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_6900. Immune System.
SignaLinkP09038.

Gene expression databases

ArrayExpressP09038.
BgeeP09038.
CleanExHS_FGF2.
GenevestigatorP09038.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR028223. FGF2.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF13. PTHR11486:SF13. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
PRINTSPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09038.
GeneWikiBasic_fibroblast_growth_factor.
GenomeRNAi2247.
NextBio9095.
PROP09038.
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, Q9UCS5, Q9UCS6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 13, 2009
Last modified: April 16, 2014
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 4

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