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Protein

Fibroblast growth factor 2

Gene

FGF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro.2 Publications

pH dependencei

Retains almost half of its activity after treatment at pH 2.0 for 3 hours at 20 degrees Celsius.1 Publication

Temperature dependencei

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei169 – 1691HeparinBy similarity

GO - Molecular functioni

  • chemoattractant activity Source: BHF-UCL
  • cytokine activity Source: BHF-UCL
  • fibroblast growth factor receptor binding Source: MGI
  • growth factor activity Source: BHF-UCL
  • heparin binding Source: UniProtKB-KW
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • activation of MAPK activity Source: ProtInc
  • branching involved in ureteric bud morphogenesis Source: UniProtKB
  • cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • chemotaxis Source: ProtInc
  • chondroblast differentiation Source: UniProtKB
  • embryonic morphogenesis Source: DFLAT
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • extracellular matrix organization Source: Reactome
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • growth factor dependent regulation of skeletal muscle satellite cell proliferation Source: AgBase
  • hyaluronan catabolic process Source: UniProtKB
  • innate immune response Source: Reactome
  • inositol phosphate biosynthetic process Source: DFLAT
  • insulin receptor signaling pathway Source: Reactome
  • negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • negative regulation of cell death Source: UniProtKB
  • negative regulation of fibroblast migration Source: UniProtKB
  • negative regulation of wound healing Source: UniProtKB
  • nervous system development Source: ProtInc
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • organ morphogenesis Source: ProtInc
  • phosphatidylinositol biosynthetic process Source: DFLAT
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive chemotaxis Source: GOC
  • positive regulation of angiogenesis Source: DFLAT
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of cell fate specification Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of endothelial cell chemotaxis to fibroblast growth factor Source: UniProtKB
  • positive regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase activity Source: DFLAT
  • positive regulation of phospholipase C activity Source: DFLAT
  • positive regulation of sprouting angiogenesis Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • Ras protein signal transduction Source: ProtInc
  • regulation of angiogenesis Source: DFLAT
  • regulation of endothelial cell chemotaxis to fibroblast growth factor Source: UniProtKB
  • release of sequestered calcium ion into cytosol Source: DFLAT
  • signal transduction Source: ProtInc
  • somatic stem cell maintenance Source: Reactome
  • wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163942. Syndecan interactions.
REACT_264617. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9400. FGFR1b ligand binding and activation.
REACT_9413. FGFR2c ligand binding and activation.
REACT_9416. FGFR2b ligand binding and activation.
REACT_9452. FGFR4 ligand binding and activation.
REACT_9510. FGFR3c ligand binding and activation.
REACT_9515. FGFR1c ligand binding and activation.
REACT_976. PI3K Cascade.
SignaLinkiP09038.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:FGF2
Synonyms:FGFB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3676. FGF2.

Subcellular locationi

  • 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.

GO - Cellular componenti

  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28115.

Chemistry

DrugBankiDB00686. Pentosan Polysulfate.
DB00877. Sirolimus.
DB00364. Sucralfate.

Polymorphism and mutation databases

BioMutaiFGF2.
DMDMi261260095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 142142Or 93, or 124, or 125, or 131, or 161PRO_0000008932Add
BLAST
Chaini143 – 288146Fibroblast growth factor 2PRO_0000008933Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Omega-N-methylarginine; alternateBy similarity
Modified residuei108 – 1081Symmetric dimethylarginine; alternateBy similarity
Modified residuei110 – 1101Omega-N-methylarginine; alternateBy similarity
Modified residuei110 – 1101Symmetric dimethylarginine; alternateBy similarity
Modified residuei112 – 1121Omega-N-methylarginine; alternateBy similarity
Modified residuei112 – 1121Symmetric dimethylarginine; alternateBy similarity
Modified residuei215 – 2151Phosphotyrosine; by TEC1 Publication

Post-translational modificationi

Phosphorylation at Tyr-215 regulates FGF2 unconventional secretion.1 Publication
Several N-termini starting at positions 94, 125, 126, 132, 143 and 162 have been identified by direct sequencing.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP09038.
PaxDbiP09038.
PRIDEiP09038.

PTM databases

PhosphoSiteiP09038.

Expressioni

Tissue specificityi

Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non-cancerous liver tissue.2 Publications

Gene expression databases

BgeeiP09038.
CleanExiHS_FGF2.
ExpressionAtlasiP09038. baseline and differential.
GenevestigatoriP09038.

Organism-specific databases

HPAiCAB000125.

Interactioni

Subunit structurei

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 FGF2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP1P294662EBI-977447,EBI-516667
FGFBP1Q145123EBI-977447,EBI-953742
FGFR1P113624EBI-977447,EBI-1028277
FGFR1P11362-142EBI-977447,EBI-6622185
FGFR2P218023EBI-977447,EBI-1028658

Protein-protein interaction databases

BioGridi108538. 21 interactions.
DIPiDIP-4012N.
IntActiP09038. 8 interactions.
MINTiMINT-222469.

Structurei

Secondary structure

1
288
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi136 – 1394Combined sources
Beta strandi151 – 1533Combined sources
Helixi156 – 1605Combined sources
Beta strandi163 – 1675Combined sources
Turni168 – 1703Combined sources
Beta strandi173 – 1764Combined sources
Beta strandi182 – 1865Combined sources
Helixi191 – 1933Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi204 – 2096Combined sources
Turni210 – 2134Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi224 – 2296Combined sources
Helixi232 – 2343Combined sources
Beta strandi236 – 2405Combined sources
Helixi242 – 2443Combined sources
Beta strandi246 – 2538Combined sources
Beta strandi264 – 2663Combined sources
Helixi269 – 2713Combined sources
Helixi277 – 2793Combined sources
Beta strandi281 – 2844Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4OEEX-ray1.50A134-288[»]
4OEFX-ray1.80A134-288[»]
4OEGX-ray1.60A134-288[»]
ProteinModelPortaliP09038.
SMRiP09038. Positions 134-288.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09038.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 27717Heparin-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi179 – 1813Cell attachment site; atypicalSequence Analysis
Motifi221 – 2233Cell attachment site; atypicalSequence Analysis

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG325757.
GeneTreeiENSGT00730000110923.
HOVERGENiHBG107917.
InParanoidiP09038.
KOiK18497.
OrthoDBiEOG7992S1.
PhylomeDBiP09038.
TreeFamiTF317805.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028223. FGF2.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF68. PTHR11486:SF68. 1 hit.
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P09038-4) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVGVGGGDVE DVTPRPGGCQ ISGRGARGCN GIPGAAAWEA ALPRRRPRRH
60 70 80 90 100
PSVNPRSRAA GSPRTRGRRT EERPSGSRLG DRGRGRALPG GRLGGRGRGR
110 120 130 140 150
APERVGGRGR GRGTAAPRAA PAARGSRPGP AGTMAAGSIT TLPALPEDGG
160 170 180 190 200
SGAFPPGHFK DPKRLYCKNG GFFLRIHPDG RVDGVREKSD PHIKLQLQAE
210 220 230 240 250
ERGVVSIKGV CANRYLAMKE DGRLLASKCV TDECFFFERL ESNNYNTYRS
260 270 280
RKYTSWYVAL KRTGQYKLGS KTGPGQKAIL FLPMSAKS

Note: Starts at an alternative CUG codon.

Length:288
Mass (Da):30,770
Last modified:October 13, 2009 - v3
Checksum:iEAE98552A39D5E19
GO
Isoform 2 (identifier: P09038-1) [UniParc]FASTAAdd to basket

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.

Show »
Length:210
Mass (Da):22,623
Checksum:iA21C7A6E82E4F5BD
GO
Isoform 3 (identifier: P09038-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Show »
Length:155
Mass (Da):17,254
Checksum:iBE6CE13373007129
GO
Isoform 4 (identifier: P09038-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:196
Mass (Da):21,203
Checksum:iD6B5447137E60343
GO

Sequence cautioni

The sequence AAA52448.1 differs from that shown. Reason: Frameshift at positions 25, 82, 98 and 133. Curated
The sequence AAB21432.2 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAB21432.2 differs from that shown. Reason: Frameshift at position 25. Curated
The sequence ABO43041.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence ABO43041.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA28027.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA28027.1 differs from that shown. Reason: Frameshift at positions 25 and 102. Curated
The sequence CAA73868.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA73868.1 differs from that shown. Reason: Frameshift at position 25. Curated
The sequence EAX05222.1 differs from that shown.Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence EAX05222.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251G → R in AAA52448 (PubMed:2435575).Curated
Sequence conflicti50 – 501H → Q in AAA52448 (PubMed:2435575).Curated
Sequence conflicti59 – 591A → R in AAA52448 (PubMed:2435575).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 3. 2 PublicationsVSP_037383Add
BLAST
Alternative sequencei1 – 9292Missing in isoform 4. 1 PublicationVSP_037384Add
BLAST
Alternative sequencei1 – 7878Missing in isoform 2. 1 PublicationVSP_038236Add
BLAST
Alternative sequencei79 – 791L → M in isoform 2. 1 PublicationVSP_038237
Alternative sequencei93 – 931L → M in isoform 4. 1 PublicationVSP_037385

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34059.1. [P09038-4]
PIRiA32398.
RefSeqiNP_001997.5. NM_002006.4. [P09038-4]
UniGeneiHs.284244.

Genome annotation databases

EnsembliENST00000608478; ENSP00000477134; ENSG00000138685. [P09038-2]
GeneIDi2247.
KEGGihsa:2247.
UCSCiuc003iev.1. human. [P09038-4]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34059.1. [P09038-4]
PIRiA32398.
RefSeqiNP_001997.5. NM_002006.4. [P09038-4]
UniGeneiHs.284244.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4OEEX-ray1.50A134-288[»]
4OEFX-ray1.80A134-288[»]
4OEGX-ray1.60A134-288[»]
ProteinModelPortaliP09038.
SMRiP09038. Positions 134-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108538. 21 interactions.
DIPiDIP-4012N.
IntActiP09038. 8 interactions.
MINTiMINT-222469.

Chemistry

BindingDBiP09038.
ChEMBLiCHEMBL3107.
DrugBankiDB00686. Pentosan Polysulfate.
DB00877. Sirolimus.
DB00364. Sucralfate.

PTM databases

PhosphoSiteiP09038.

Polymorphism and mutation databases

BioMutaiFGF2.
DMDMi261260095.

Proteomic databases

MaxQBiP09038.
PaxDbiP09038.
PRIDEiP09038.

Protocols and materials databases

DNASUi2247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000608478; ENSP00000477134; ENSG00000138685. [P09038-2]
GeneIDi2247.
KEGGihsa:2247.
UCSCiuc003iev.1. human. [P09038-4]

Organism-specific databases

CTDi2247.
GeneCardsiGC04P123747.
HGNCiHGNC:3676. FGF2.
HPAiCAB000125.
MIMi134920. gene.
neXtProtiNX_P09038.
PharmGKBiPA28115.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG325757.
GeneTreeiENSGT00730000110923.
HOVERGENiHBG107917.
InParanoidiP09038.
KOiK18497.
OrthoDBiEOG7992S1.
PhylomeDBiP09038.
TreeFamiTF317805.

Enzyme and pathway databases

ReactomeiREACT_110235. Phospholipase C-mediated cascade: FGFR1.
REACT_120863. Activated point mutants of FGFR2.
REACT_121153. Signaling by activated point mutants of FGFR1.
REACT_121249. FGFR3 mutant receptor activation.
REACT_121337. Signaling by activated point mutants of FGFR3.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163942. Syndecan interactions.
REACT_264617. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355146. Phospholipase C-mediated cascade, FGFR2.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355194. SHC-mediated cascade:FGFR1.
REACT_355197. SHC-mediated cascade:FGFR3.
REACT_355202. Signaling by FGFR4 mutants.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355216. Phospholipase C-mediated cascade, FGFR4.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355221. Signaling by FGFR1 mutants.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355313. Signaling by FGFR3 mutants.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355511. Signaling by FGFR2 mutants.
REACT_355514. Phospholipase C-mediated cascade, FGFR3.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_9400. FGFR1b ligand binding and activation.
REACT_9413. FGFR2c ligand binding and activation.
REACT_9416. FGFR2b ligand binding and activation.
REACT_9452. FGFR4 ligand binding and activation.
REACT_9510. FGFR3c ligand binding and activation.
REACT_9515. FGFR1c ligand binding and activation.
REACT_976. PI3K Cascade.
SignaLinkiP09038.

Miscellaneous databases

ChiTaRSiFGF2. human.
EvolutionaryTraceiP09038.
GeneWikiiBasic_fibroblast_growth_factor.
GenomeRNAii2247.
NextBioi9095.
PROiP09038.
SOURCEiSearch...

Gene expression databases

BgeeiP09038.
CleanExiHS_FGF2.
ExpressionAtlasiP09038. baseline and differential.
GenevestigatoriP09038.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028223. FGF2.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF68. PTHR11486:SF68. 1 hit.
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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. 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.

Entry informationi

Entry nameiFGF2_HUMAN
AccessioniPrimary (citable) accession number: P09038
Secondary accession number(s): A4LBB8
, O00527, P78443, Q16443, Q5PY50, Q7KZ11, Q7KZ72, Q9UC54, Q9UCS5, Q9UCS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 13, 2009
Last modified: May 27, 2015
This is version 189 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

This protein binds heparin more strongly than does aFGF.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.