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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. Can induce angiogenesis (PubMed:23469107).3 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)DescriptionActionsGraphical viewLength
Binding sitei169HeparinBy similarity1

GO - Molecular functioni

  • 1-phosphatidylinositol-3-kinase activity Source: Reactome
  • 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
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • protein tyrosine kinase activity Source: Reactome
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome

GO - Biological processi

  • activation of MAPK activity Source: ProtInc
  • animal organ morphogenesis 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
  • extracellular matrix organization 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
  • inositol phosphate biosynthetic process Source: DFLAT
  • MAPK cascade 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
  • phosphatidylinositol biosynthetic process Source: DFLAT
  • phosphatidylinositol-mediated signaling Source: Reactome
  • 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
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • release of sequestered calcium ion into cytosol Source: DFLAT
  • signal transduction Source: ProtInc
  • somatic stem cell population 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

BioCyciZFISH:ENSG00000138685-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1839122. Signaling by activated point mutants of FGFR1.
R-HSA-1839130. Signaling by activated point mutants of FGFR3.
R-HSA-190322. FGFR4 ligand binding and activation.
R-HSA-190370. FGFR1b ligand binding and activation.
R-HSA-190372. FGFR3c ligand binding and activation.
R-HSA-190373. FGFR1c ligand binding and activation.
R-HSA-190375. FGFR2c ligand binding and activation.
R-HSA-190377. FGFR2b ligand binding and activation.
R-HSA-2033514. FGFR3 mutant receptor activation.
R-HSA-2033519. Activated point mutants of FGFR2.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-2892247. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-5654219. Phospholipase C-mediated cascade: FGFR1.
R-HSA-5654221. Phospholipase C-mediated cascade, FGFR2.
R-HSA-5654227. Phospholipase C-mediated cascade, FGFR3.
R-HSA-5654228. Phospholipase C-mediated cascade, FGFR4.
R-HSA-5654687. Downstream signaling of activated FGFR1.
R-HSA-5654688. SHC-mediated cascade:FGFR1.
R-HSA-5654689. PI-3K cascade:FGFR1.
R-HSA-5654693. FRS-mediated FGFR1 signaling.
R-HSA-5654695. PI-3K cascade:FGFR2.
R-HSA-5654699. SHC-mediated cascade:FGFR2.
R-HSA-5654700. FRS-mediated FGFR2 signaling.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654710. PI-3K cascade:FGFR3.
R-HSA-5654712. FRS-mediated FGFR4 signaling.
R-HSA-5654719. SHC-mediated cascade:FGFR4.
R-HSA-5654720. PI-3K cascade:FGFR4.
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-5658623. FGFRL1 modulation of FGFR1 signaling.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP09038.
SIGNORiP09038.

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
Proteomesi
  • UP000005640 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: MGI
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi2247.
OpenTargetsiENSG00000138685.
PharmGKBiPA28115.

Chemistry databases

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

Polymorphism and mutation databases

BioMutaiFGF2.
DMDMi261260095.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000089321 – 142Or 93, or 124, or 125, or 131, or 161Add BLAST142
ChainiPRO_0000008933143 – 288Fibroblast growth factor 2Add BLAST146

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei108Omega-N-methylarginine; alternateBy similarity1
Modified residuei108Symmetric dimethylarginine; alternateBy similarity1
Modified residuei110Omega-N-methylarginine; alternateBy similarity1
Modified residuei110Symmetric dimethylarginine; alternateBy similarity1
Modified residuei112Omega-N-methylarginine; alternateBy similarity1
Modified residuei112Symmetric dimethylarginine; alternateBy similarity1
Modified residuei215Phosphotyrosine; by TEC1 Publication1
Cross-linki228Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources

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

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP09038.
PaxDbiP09038.
PeptideAtlasiP09038.
PRIDEiP09038.

PTM databases

iPTMnetiP09038.
PhosphoSitePlusiP09038.

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

BgeeiENSG00000138685.
CleanExiHS_FGF2.
ExpressionAtlasiP09038. baseline and differential.
GenevisibleiP09038. HS.

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. Interacts with FGFBP3 (PubMed:18669637).9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP1P294662EBI-977447,EBI-516667
FGFBP1Q145123EBI-977447,EBI-953742
FGFR1P113625EBI-977447,EBI-1028277
FGFR1P11362-142EBI-977447,EBI-6622185
FGFR2P218023EBI-977447,EBI-1028658
PTX3P2602216EBI-977447,EBI-11574553

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • fibroblast growth factor receptor binding Source: MGI
  • growth factor activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi108538. 24 interactors.
DIPiDIP-4012N.
IntActiP09038. 11 interactors.
MINTiMINT-222469.
STRINGi9606.ENSP00000264498.

Chemistry databases

BindingDBiP09038.

Structurei

Secondary structure

1288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi136 – 139Combined sources4
Beta strandi151 – 153Combined sources3
Helixi156 – 160Combined sources5
Beta strandi163 – 167Combined sources5
Turni168 – 170Combined sources3
Beta strandi173 – 176Combined sources4
Beta strandi182 – 186Combined sources5
Helixi191 – 193Combined sources3
Beta strandi195 – 201Combined sources7
Beta strandi204 – 209Combined sources6
Turni210 – 213Combined sources4
Beta strandi214 – 218Combined sources5
Beta strandi220 – 222Combined sources3
Beta strandi224 – 229Combined sources6
Helixi232 – 234Combined sources3
Beta strandi236 – 240Combined sources5
Helixi242 – 244Combined sources3
Beta strandi246 – 253Combined sources8
Beta strandi264 – 266Combined sources3
Helixi269 – 271Combined sources3
Helixi277 – 279Combined sources3
Beta strandi281 – 284Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09038.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni261 – 277Heparin-bindingBy similarityAdd BLAST17

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi179 – 181Cell attachment site; atypicalSequence analysis3
Motifi221 – 223Cell attachment site; atypicalSequence analysis3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00730000110923.
HOVERGENiHBG107917.
InParanoidiP09038.
KOiK18497.
PhylomeDBiP09038.
TreeFamiTF317805.

Family and domain databases

CDDicd00058. FGF. 1 hit.
InterProiIPR008996. Cytokine_IL1-like.
IPR028223. FGF2.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF83. PTHR11486:SF83. 1 hit.
PfamiPF00167. FGF. 1 hit.
[Graphical view]
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 differs from that shown. Reason: Frameshift at positions 25, 82, 98 and 133.Curated
The sequence AAB21432 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAB21432 differs from that shown. Reason: Frameshift at position 25.Curated
The sequence ABO43041 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence ABO43041 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA28027 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA28027 differs from that shown. Reason: Frameshift at positions 25 and 102.Curated
The sequence CAA73868 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA73868 differs from that shown. Reason: Frameshift at position 25.Curated
The sequence EAX05222 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence EAX05222 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25G → R in AAA52448 (PubMed:2435575).Curated1
Sequence conflicti50H → Q in AAA52448 (PubMed:2435575).Curated1
Sequence conflicti59A → R in AAA52448 (PubMed:2435575).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0373831 – 133Missing in isoform 3. 2 PublicationsAdd BLAST133
Alternative sequenceiVSP_0373841 – 92Missing in isoform 4. 1 PublicationAdd BLAST92
Alternative sequenceiVSP_0382361 – 78Missing in isoform 2. 1 PublicationAdd BLAST78
Alternative sequenceiVSP_03823779L → M in isoform 2. 1 Publication1
Alternative sequenceiVSP_03738593L → M in isoform 4. 1 Publication1

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.
UCSCiuc062zki.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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108538. 24 interactors.
DIPiDIP-4012N.
IntActiP09038. 11 interactors.
MINTiMINT-222469.
STRINGi9606.ENSP00000264498.

Chemistry databases

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

PTM databases

iPTMnetiP09038.
PhosphoSitePlusiP09038.

Polymorphism and mutation databases

BioMutaiFGF2.
DMDMi261260095.

Proteomic databases

EPDiP09038.
PaxDbiP09038.
PeptideAtlasiP09038.
PRIDEiP09038.

Protocols and materials databases

DNASUi2247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000608478; ENSP00000477134; ENSG00000138685. [P09038-2]
GeneIDi2247.
KEGGihsa:2247.
UCSCiuc062zki.1. human. [P09038-4]

Organism-specific databases

CTDi2247.
DisGeNETi2247.
GeneCardsiFGF2.
HGNCiHGNC:3676. FGF2.
HPAiCAB000125.
MIMi134920. gene.
neXtProtiNX_P09038.
OpenTargetsiENSG00000138685.
PharmGKBiPA28115.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00730000110923.
HOVERGENiHBG107917.
InParanoidiP09038.
KOiK18497.
PhylomeDBiP09038.
TreeFamiTF317805.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138685-MONOMER.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1839122. Signaling by activated point mutants of FGFR1.
R-HSA-1839130. Signaling by activated point mutants of FGFR3.
R-HSA-190322. FGFR4 ligand binding and activation.
R-HSA-190370. FGFR1b ligand binding and activation.
R-HSA-190372. FGFR3c ligand binding and activation.
R-HSA-190373. FGFR1c ligand binding and activation.
R-HSA-190375. FGFR2c ligand binding and activation.
R-HSA-190377. FGFR2b ligand binding and activation.
R-HSA-2033514. FGFR3 mutant receptor activation.
R-HSA-2033519. Activated point mutants of FGFR2.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-2892247. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-5654219. Phospholipase C-mediated cascade: FGFR1.
R-HSA-5654221. Phospholipase C-mediated cascade, FGFR2.
R-HSA-5654227. Phospholipase C-mediated cascade, FGFR3.
R-HSA-5654228. Phospholipase C-mediated cascade, FGFR4.
R-HSA-5654687. Downstream signaling of activated FGFR1.
R-HSA-5654688. SHC-mediated cascade:FGFR1.
R-HSA-5654689. PI-3K cascade:FGFR1.
R-HSA-5654693. FRS-mediated FGFR1 signaling.
R-HSA-5654695. PI-3K cascade:FGFR2.
R-HSA-5654699. SHC-mediated cascade:FGFR2.
R-HSA-5654700. FRS-mediated FGFR2 signaling.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654710. PI-3K cascade:FGFR3.
R-HSA-5654712. FRS-mediated FGFR4 signaling.
R-HSA-5654719. SHC-mediated cascade:FGFR4.
R-HSA-5654720. PI-3K cascade:FGFR4.
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-5658623. FGFRL1 modulation of FGFR1 signaling.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP09038.
SIGNORiP09038.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000138685.
CleanExiHS_FGF2.
ExpressionAtlasiP09038. baseline and differential.
GenevisibleiP09038. HS.

Family and domain databases

CDDicd00058. FGF. 1 hit.
InterProiIPR008996. Cytokine_IL1-like.
IPR028223. FGF2.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF83. PTHR11486:SF83. 1 hit.
PfamiPF00167. FGF. 1 hit.
[Graphical view]
PRINTSiPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 205 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

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 one 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.