Q60487 (FGF2_CAVPO) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 84. History...
Names and origin
|Protein names||Recommended name:|
Fibroblast growth factor 2
Basic fibroblast growth factor
Heparin-binding growth factor 2
Prostatic growth factor
|Organism||Cavia porcellus (Guinea pig) [Reference proteome]|
|Taxonomic identifier||10141 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia|
|Sequence length||170 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro By similarity.
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 By similarity.
Secreted By similarity. Nucleus By similarity. Note: Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism. Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane By similarity. 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 By similarity.
The N-terminus of isoform 2 is blocked Probable.
Phosphorylation at Tyr-97 regulates FGF2 unconventional secretion By similarity.
Belongs to the heparin-binding growth factors family.
The sequence AAA85394.1 differs from that shown. Reason: Frameshift at positions 77, 88, 93 and 149. The correction of the frameshifts allows to extend the similarity to the human sequence and is based on partial amino-acid sequencing.
|This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]|
|Isoform 1 (identifier: Q60487-1) |
Also known as: 25 kDa;
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.
|Isoform 2 (identifier: Q60487-2) |
Also known as: 18 kDa;
The sequence of this isoform differs from the canonical sequence as follows:
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||‹1 – 170||›170||Fibroblast growth factor 2||PRO_0000008930|
|Region||143 – 159||17||Heparin-binding By similarity|
|Binding site||51||1||Heparin By similarity|
Amino acid modifications
|Modified residue||4||1||Omega-N-methylarginine; alternate Ref.3|
|Modified residue||4||1||Symmetric dimethylarginine; alternate Ref.3|
|Modified residue||6||1||Omega-N-methylarginine; alternate Ref.3|
|Modified residue||6||1||Symmetric dimethylarginine; alternate Ref.3|
|Modified residue||8||1||Omega-N-methylarginine; alternate Ref.3|
|Modified residue||8||1||Symmetric dimethylarginine; alternate Ref.3|
|Modified residue||97||1||Phosphotyrosine; by TEC By similarity|
|Alternative sequence||‹1 – 21||›21||Missing in isoform 2.||VSP_018726|
|Non-adjacent residues||15 – 16||2|
|Non-adjacent residues||50 – 51||2|
|||"An amino-terminally extended and post-translationally modified form of a 25kD basic fibroblast growth factor."|
Sommer A., Moscatelli D., Rifkin D.B.
Biochem. Biophys. Res. Commun. 160:1267-1274(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, ALTERNATIVE INITIATION.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-170.
|||"Direct evidence for methylation of arginine residues in high molecular weight forms of basic fibroblast growth factor."|
Burgess W.H., Bizik J., Mehlman T., Quarto N., Rifkin D.B.
Cell Regul. 2:87-93(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, METHYLATION AT ARG-4; ARG-6 AND ARG-8.
|||"Mr 25,000 heparin-binding protein from guinea pig brain is a high molecular weight form of basic fibroblast growth factor."|
Moscatelli D., Joseph-Silverstein J., Manejias R., Rifkin D.B.
Proc. Natl. Acad. Sci. U.S.A. 84:5778-5782(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
|L75974 mRNA. Translation: AAA85394.1. Frameshift.|
3D structure databases
|SMR||Q60487. Positions 22-170. |
Protein-protein interaction databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR008996. Cytokine_IL1-like. |
|PANTHER||PTHR11486. PTHR11486. 1 hit. |
|Pfam||PF00167. FGF. 1 hit. |
|PRINTS||PR00263. HBGFFGF. |
|SMART||SM00442. FGF. 1 hit. |
|SUPFAM||SSF50353. Cytok_IL1_like. 1 hit. |
|PROSITE||PS00247. HBGF_FGF. 1 hit. |
|Accession||Primary (citable) accession number: Q60487|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|
Index of protein domains and families