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Protein Page:
FGF2 (mouse)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
FGF2 Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro. 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. Expressed in granulosa and cumulus cells. Expressed in hepatocellular carcinoma cells, but not in non- cancerous liver tissue. Belongs to the heparin-binding growth factors family. 4 isoforms of the human protein are produced by alternative initiation. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Activator protein
Cellular Component: extracellular space; cytoplasm; extracellular region; nucleus; cytosol
Molecular Function: heparin binding; protein binding; ligand-dependent nuclear receptor transcription coactivator activity; growth factor activity; cytokine activity; fibroblast growth factor receptor binding; receptor binding; chemoattractant activity
Biological Process: activation of MAPKK activity; regulation of cell cycle; positive regulation of transcription, DNA-dependent; positive regulation of smooth muscle cell proliferation; multicellular organismal development; adrenocorticotropin hormone secreting cell differentiation; thyroid stimulating hormone secreting cell differentiation; cardiac muscle cell proliferation; hyaluronan catabolic process; embryonic development ending in birth or egg hatching; negative regulation of cell proliferation; substantia nigra development; glial cell differentiation; positive chemotaxis; induction of an organ; positive regulation of cell proliferation; regulation of retinal cell programmed cell death; angiogenesis; response to axon injury; cell differentiation; positive regulation of granule cell precursor proliferation; positive regulation of cardiac muscle cell proliferation; fibroblast growth factor receptor signaling pathway; positive regulation of cell fate specification; positive regulation of blood vessel endothelial cell migration; positive regulation of phosphoinositide 3-kinase activity; negative regulation of blood vessel endothelial cell migration; positive regulation of protein kinase B signaling cascade; positive regulation of osteoblast differentiation; stem cell development; positive regulation of angiogenesis; cell migration during sprouting angiogenesis; ureteric bud branching; positive regulation of cell division; release of sequestered calcium ion into cytosol; phosphatidylinositol biosynthetic process; positive regulation of endothelial cell proliferation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of protein amino acid phosphorylation; positive regulation of cell differentiation; inositol phosphate biosynthetic process; positive regulation of epithelial cell proliferation; lung development
Reference #:  P15655 (UniProtKB)
Alt. Names/Synonyms: Basic fibroblast growth factor; BFGF; Fgf-2; Fgf2; Fgfb; fibroblast growth factor 2; HBGF-2; Heparin-binding growth factor 2
Gene Symbols: Fgf2
Molecular weight: 17,153 Da
Basal Isoelectric point: 9.58  Predict pI for various phosphorylation states
Select Structure to View Below

FGF2

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: Y81‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       mouse

 
0 1 - gap
0 1 - gap
1 0 - gap
1 0 - gap
1 0 - gap
1 0 - gap
1 0 - gap
1 0 - gap
1 0 - gap
1 0 - gap
0 1 S4 ____MAASGITSLPA
0 1 S8 MAASGITSLPALPED
2 0 K34 DPKRLYCKNGGFFLR
1 0 S72 AEERGVVSIKGVCAN
1 0 Y81-p KGVCANRyLAMKEDG
0 1 K94 DGRLLASKCVTEECF
1 2 Y111-p ERLESNNyNTYRSRK
1 0 S116 NNyNTYRSRKYSSWy
0 1 Y119 NTYRSRKYSSWyVAL
1 1 S120 TYRSRKYSSWyVALK
1 0 Y123-p SRKYSSWyVALKRTG
2 0 K127 SSWyVALKRTGQYKL
1 0 K133 LKRTGQYKLGSKTGP
1 0 K137 GQYKLGSKTGPGQKA
2 0 K143 SKTGPGQKAILFLPM
0 1 S151 AILFLPMSAKS____
0 1 S154 FLPMSAKS_______
  human

 
S62-p PRSRAAGsPRtRGRR
T65-p RAAGsPRtRGRRTEE
R82-m2 SGSRLGDrGrGrALP
R84-m2 SRLGDrGrGrALPGG
R86-m2 LGDrGrGrALPGGRL
R96-m2 PGGRLGGrGrGRAPE
R98-m2 GRLGGrGrGRAPERV
R108-m2 APERVGGrGrGrGTA
R110-m2 ERVGGrGrGrGTAAP
R112-m2 VGGrGrGrGTAAPRA
S138-p AGTMAAGsITtLPAL
T141-p MAAGsITtLPALPED
K168-ac DPKRLYCkNGGFFLR
S206-p AEERGVVsIKGVCAN
Y215 KGVCANRYLAMKEDG
K228-ub DGRLLASkCVTDECF
Y245-p ERLESNNyNTYRsRK
S250-p NNyNTYRsRKytSWY
Y253-p NTYRsRKytSWYVAL
T254-p TYRsRKytSWYVALk
Y257 sRKytSWYVALkRTG
K261-ac tSWYVALkRTGQYkL
K267-ac LkRTGQYkLGSkTGP
K271-ac GQYkLGSkTGPGQkA
K277-ac SkTGPGQkAILFLPM
S285-p AILFLPMsAKs____
S288-p FLPMsAKs_______
  rat

 
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
S5 ___MAAGSITSLPAL
S8 MAAGSITSLPALPED
K34 DPKRLYCKNGGFFLR
S72 AEERGVVSIKGVCAN
Y81 KGVCANRYLAMKEDG
K94 DGRLLASKCVTEECF
Y111 ERLESNNYNTYRSRK
S116 NNYNTYRSRKYSSWY
Y119 NTYRSRKYSSWYVAL
S120 TYRSRKYSSWYVALK
Y123 SRKYSSWYVALKRTG
K127 SSWYVALKRTGQYKL
K133 LKRTGQYKLGSKTGP
K137 GQYKLGSKTGPGQKA
K143 SKTGPGQKAILFLPM
S151 AILFLPMSAKS____
S154 FLPMSAKS_______
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