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Protein

Fibroblast growth factor 2

Gene

FGF2

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511HeparinBy similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. branching involved in ureteric bud morphogenesis Source: UniProtKB
  3. cell differentiation Source: UniProtKB-KW
  4. fibroblast growth factor receptor signaling pathway Source: InterPro
  5. negative regulation of cell death Source: UniProtKB
  6. positive regulation of cell division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Growth factor, Mitogen

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Heparin-binding

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
Prostatic growth factor
Gene namesi
Name:FGF2
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447 Componenti: Unplaced

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 170›170Fibroblast growth factor 2PRO_0000008930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Omega-N-methylarginine; alternate1 Publication
Modified residuei4 – 41Symmetric dimethylarginine; alternate1 Publication
Modified residuei6 – 61Omega-N-methylarginine; alternate1 Publication
Modified residuei6 – 61Symmetric dimethylarginine; alternate1 Publication
Modified residuei8 – 81Omega-N-methylarginine; alternate1 Publication
Modified residuei8 – 81Symmetric dimethylarginine; alternate1 Publication
Modified residuei97 – 971Phosphotyrosine; by TECBy similarity

Post-translational modificationi

The N-terminus of isoform 2 is blocked.Curated
Phosphorylation at Tyr-97 regulates FGF2 unconventional secretion.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000004847.

Structurei

3D structure databases

ProteinModelPortaliQ60487.
SMRiQ60487. Positions 22-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni143 – 15917Heparin-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG325757.
HOVERGENiHBG107917.
InParanoidiQ60487.

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 (2)i

Sequence statusi: Fragments.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q60487-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
VGGRGRGRGT AAAARREPGG AMAAGSITTL PALPEGGDGG AFAPGHFKDP
60 70 80 90 100
NGGFFLRIHP DGRVDGVREK TDPHIKLQLQ AEDRGVVSIK GVCANRYLAM
110 120 130 140 150
KEDGRLLASK CVTDECFFFE RLESNNYNTY RSRKYSSWYV ALKRTGQYKL
160 170
GSKTGPGQKA ILFLPMSAKS
Length:170
Mass (Da):18,354
Last modified:April 30, 2000 - v2
Checksum:iF36BDBC736E5FEBE
GO
Isoform 2 (identifier: Q60487-2) [UniParc]FASTAAdd to basket

Also known as: 18 kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.

Show »
Length:149
Mass (Da):16,392
Checksum:i7A246D9C9C806B87
GO

Sequence cautioni

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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi15 – 162Curated
Non-adjacent residuesi50 – 512Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei‹1 – 21›21Missing in isoform 2. CuratedVSP_018726Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L75974 mRNA. Translation: AAA85394.1. Frameshift.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L75974 mRNA. Translation: AAA85394.1. Frameshift.

3D structure databases

ProteinModelPortaliQ60487.
SMRiQ60487. Positions 22-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000004847.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiNOG325757.
HOVERGENiHBG107917.
InParanoidiQ60487.

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

  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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, ALTERNATIVE INITIATION.
  2. Ricciardelli C.
    Submitted (DEC-1995) 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(1990) [PubMed] [Europe PMC] [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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Tissue: Brain.

Entry informationi

Entry nameiFGF2_CAVPO
AccessioniPrimary (citable) accession number: Q60487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2004
Last sequence update: April 30, 2000
Last modified: January 6, 2015
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.