Q60487 (FGF2_CAVPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 19, 2011.
Version 75.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Heparin-binding growth factor 2 Short name=HBGF-2 Alternative name(s): Basic fibroblast growth factor Short name=bFGF Fibroblast growth factor 2 Short name=FGF-2 Prostatic growth factor | ||
| Gene names |
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| Organism | Cavia porcellus (Guinea pig) | ||
| Taxonomic identifier | 10141 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia |
Protein attributes
| Sequence length | 170 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence 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 By similarity. |
| 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 By similarity. |
| Subcellular location | Secreted 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. |
| Post-translational modification | The N-terminus of isoform 2 is blocked Probable. Phosphorylation at Tyr-97 regulates FGF2 unconventional secretion By similarity. |
| Sequence similarities | Belongs to the heparin-binding growth factors family. |
| Sequence caution | 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Angiogenesis Differentiation |
| Cellular component | Secreted |
| Coding sequence diversity | Alternative initiation |
| Ligand | Heparin-binding |
| Molecular function | Developmental protein Growth factor Mitogen |
| PTM | Methylation Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | branching involved in ureteric bud morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell deathInferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell divisionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW heparin bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| 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: 1-21: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 170 | ›170 | Heparin-binding growth factor 2 | PRO_0000008930 | |||||
Regions | |||||||||
| Region | 143 – 159 | 17 | Heparin-binding By similarity | ||||||
Sites | |||||||||
| 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 | ||||||
Natural variations | |||||||||
| Alternative sequence | ‹1 – 21 | ›21 | Missing in isoform 2. | VSP_018726 | |||||
Experimental info | |||||||||
| Non-adjacent residues | 15 – 16 | 2 | |||||||
| Non-adjacent residues | 50 – 51 | 2 | |||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "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: 2730645] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, ALTERNATIVE INITIATION. |
| [2] | Ricciardelli C. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-170. Tissue: Prostate. |
| [3] | "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: 1713785] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, METHYLATION AT ARG-4; ARG-6 AND ARG-8. |
| [4] | "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: 3475702] [Abstract] Cited for: CHARACTERIZATION. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L75974 mRNA. Translation: AAA85394.1. Frameshift. |
3D structure databases | |
| ProteinModelPortal | Q60487. |
| SMR | Q60487. Positions 22-170. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q60487. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSCPOT00000005443; ENSCPOP00000004847; ENSCPOG00000005386. |
Phylogenomic databases | |
| eggNOG | roNOG16213. |
| GeneTree | ENSGT00600000084030. |
| HOVERGEN | HBG107917. |
| InParanoid | Q60487. |
| OrthoDB | EOG4K0QPR. |
Family and domain databases | |
| InterPro | IPR008996. Cytokine_IL1-like. IPR002209. GF_heparin-bd. IPR002348. IL1_HBGF. [Graphical view] |
| PANTHER | PTHR11486. IL1_HBGF. 1 hit. |
| Pfam | PF00167. FGF. 1 hit. [Graphical view] |
| PRINTS | PR00263. HBGFFGF. PR00262. IL1HBGF. |
| SMART | SM00442. FGF. 1 hit. [Graphical view] |
| SUPFAM | SSF50353. Cytok_IL1_like. 1 hit. |
| PROSITE | PS00247. HBGF_FGF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FGF2_CAVPO | ||||||||
| Accession | Primary (citable) accession number: Q60487 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with