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IID00438
 UniprotP09038
ProteinFibroblast growth factor 2
GeneFGF2
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
288
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 134-288 Hetero dimer : IID00546Complex
 Evidence X-RAY 1iil D Reference
       Region 1iil D 134-157 disorder
       Region 1iil D 158-287 order
       Region 1iil D 288-288 disorder
 Evidence X-RAY 1iil C Reference
       Region 1iil C 134-157 disorder
       Region 1iil C 158-288 order
 Evidence X-RAY 1iil B Reference
       Region 1iil B 134-157 disorder
       Region 1iil B 158-287 order
       Region 1iil B 288-288 disorder
 Evidence X-RAY 1iil A Reference
       Region 1iil A 134-157 disorder
       Region 1iil A 158-288 order
 Evidence X-RAY 1ii4 D Reference
       Region 1ii4 D 134-153 disorder
       Region 1ii4 D 154-287 order
       Region 1ii4 D 288-288 disorder
 Evidence X-RAY 1ii4 C Reference
       Region 1ii4 C 134-153 disorder
       Region 1ii4 C 154-287 order
       Region 1ii4 C 288-288 disorder
 Evidence X-RAY 1ii4 B Reference
       Region 1ii4 B 134-153 disorder
       Region 1ii4 B 154-287 order
       Region 1ii4 B 288-288 disorder
 Evidence X-RAY 1ii4 A Reference
       Region 1ii4 A 134-153 disorder
       Region 1ii4 A 154-287 order
       Region 1ii4 A 288-288 disorder
Seq 134-288 Monomer :
 Evidence NMR 1bld A Reference
       Region 1bld A 134-161 disorder
       Region 1bld A 134-135 high_rmsd
       Region 1bld A 141-141 high_rmsd
       Region 1bld A 148-152 high_rmsd
       Region 1bld A 162-285 order
       Region 1bld A 286-288 disorder
 Evidence NMR 1bla A Reference
       Region 1bla A 134-161 disorder
       Region 1bla A 162-285 order
       Region 1bla A 286-288 order
 Evidence X-RAY 4oeg A Reference
       Region 4oeg A 134-161 disorder
       Region 4oeg A 162-285 order
       Region 4oeg A 286-288 disorder
 Evidence X-RAY 4oef A Reference
       Region 4oef A 134-160 disorder
       Region 4oef A 161-285 order
       Region 4oef A 286-288 disorder
 Evidence X-RAY 4oee A Reference
       Region 4oee A 134-153 disorder
       Region 4oee A 154-285 order
       Region 4oee A 286-288 disorder
 Evidence X-RAY 4fgf A Reference
       Region 4fgf A 143-161 disorder
       Region 4fgf A 162-285 order
       Region 4fgf A 286-288 disorder
 Evidence X-RAY 2fgf A Reference
       Region 2fgf A 143-160 disorder
       Region 2fgf A 161-286 order
       Region 2fgf A 287-288 disorder
 Evidence X-RAY 1fga A Reference
       Region 1fga A 143-161 disorder
       Region 1fga A 162-285 order
       Region 1fga A 286-288 disorder
 Evidence X-RAY 2bfh A Reference
       Region 2bfh A 161-288 order
 Evidence X-RAY 1bfg A Reference
       Region 1bfg A 143-160 disorder
       Region 1bfg A 161-286 order
       Region 1bfg A 287-288 disorder
 Evidence X-RAY 1bff A Reference
       Region 1bff A 160-288 order
 Evidence X-RAY 1bfc A Reference
       Region 1bfc A 142-161 disorder
       Region 1bfc A 162-285 order
       Region 1bfc A 286-288 disorder
 Evidence X-RAY 1bfb A Reference
       Region 1bfb A 142-161 disorder
       Region 1bfb A 162-285 order
       Region 1bfb A 286-288 disorder
 Evidence X-RAY 1bas A Reference
       Region 1bas A 135-160 disorder
       Region 1bas A 161-285 order
       Region 1bas A 286-288 disorder
Seq 143-288 Homo dimer :
 Evidence X-RAY 5x1o B Reference
       Region 5x1o B 143-159 disorder
       Region 5x1o B 160-286 order
       Region 5x1o B 287-288 disorder
 Evidence X-RAY 5x1o A Reference
       Region 5x1o A 143-159 disorder
       Region 5x1o A 160-286 order
       Region 5x1o A 287-288 disorder
Seqdisorder 154-157
 Evidence X-RAY This region is described to be disordered in wild type (1ev2) (PubMed=11390973). Reference
       Region 154-157 disorder
Seq 157-288 Hetero octamer : IID00546Complex
 Evidence X-RAY 1ev2 D Reference
       Region 1ev2 D 157-157 disorder
       Region 1ev2 D 158-287 order
       Region 1ev2 D 288-288 disorder
 Evidence X-RAY 1ev2 C Reference
       Region 1ev2 C 157-157 disorder
       Region 1ev2 C 158-287 order
       Region 1ev2 C 288-288 disorder
 Evidence X-RAY 1ev2 B Reference
       Region 1ev2 B 157-157 disorder
       Region 1ev2 B 158-287 order
       Region 1ev2 B 288-288 disorder
 Evidence X-RAY 1ev2 A Reference
       Region 1ev2 A 157-157 disorder
       Region 1ev2 A 158-287 order
       Region 1ev2 A 288-288 disorder
Seq 157-288 Hetero tetramer : IID00650Complex
 Evidence X-RAY 1fq9 B Reference
       Region 1fq9 B 157-157 disorder
       Region 1fq9 B 158-286 order
       Region 1fq9 B 287-288 disorder
 Evidence X-RAY 1fq9 A Reference
       Region 1fq9 A 157-157 disorder
       Region 1fq9 A 158-286 order
       Region 1fq9 A 287-288 disorder
 Evidence X-RAY 1cvs B Reference
       Region 1cvs B 157-157 disorder
       Region 1cvs B 158-286 order
       Region 1cvs B 287-288 disorder
 Evidence X-RAY 1cvs A Reference
       Region 1cvs A 157-157 disorder
       Region 1cvs A 158-286 order
       Region 1cvs A 287-288 disorder
Seq 161-286 Hetero tetramer : IID00410Complex
 Evidence NMR 2m49 C Reference
       Region 2m49 C 161-286 order
 Evidence NMR 2m49 A Reference
       Region 2m49 A 161-286 order
SeqProS verified 154-157 FGFR2 of 1ii4 is Ser252Trp mutant observed in Apert syndrome. The mutation causes a conformational change in FGFR2 that increases ligand binding affinity. Hetero dimer : IID00546Complex
       Region 1ii4 A 154-287 order
       Region 1ii4 B 154-287 order
       Region 1ii4 C 154-287 order
       Region 1ii4 D 154-287 order
       Region 154-157 disorder
Seqphosphorylation
    215-215 Phosphotyrosine; by TEC
 
Prediction
NeProc
Disorder 1-154,271-274,280-287
Order 155-270,275-279,288-288
ProS 1-46,102-106,136-154,271-274,280-287
AlphaFold
Disorder 1-159,288-288
Order 160-287
Pfam Hmmer
PF00167 161-282 1e-65
SEG 2-12 ,33-58 ,61-132
Function
Function in SwissProt
Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:8663044). Also acts as an integrin ligand which is required for FGF2 signaling (PubMed:28302677). Binds to integrin ITGAV:ITGB3 (PubMed:28302677). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (PubMed:8663044, PubMed:28302677). Functions as a potent mitogen in vitro (PubMed:1721615, PubMed:3964259, PubMed:3732516). Can induce angiogenesis (PubMed:23469107, PubMed:28302677). Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation (PubMed:29501879).
Biological Process
See also
Diagram with PDB data
S100B/S100BCALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES