STRINGSTRING
FIM1 FIM1 PRF1 PRF1 PRF2 PRF2 PRF5 PRF5 PRF4 PRF4 PRF3 PRF3
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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FIM1Fimbrin-1; Cross-links actin filaments (F-actin) in a calcium independent manner. Induces the formation of actin aggregates. Stabilizes and prevents F-actin depolymerization mediated by profilin. Key regulator of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. (687 aa)
PRF1Profilin-1; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. Coordinates the stochastic dynamic properties of actin filaments by modulating formin- mediated actin nucleation and assembly during axial cell expansion. Binds G-actin and poly-L-proline in vitro. Inhib [...] (131 aa)
PRF2Profilin-2; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds G- actin and poly-L-proline with low affinity in vitro. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. At high concentrations, profilin prevents the pol [...] (131 aa)
PRF5Profilin-5; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF4 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips. (134 aa)
PRF4Profilin-4; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips. (134 aa)
PRF3Profilin-3; Binds to actin monomers and regulates the organization of the actin cytoskeleton. Can increase the critical concentration (Cc) of actin assembly in vitro. Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3. PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathog [...] (168 aa)
Your Current Organism:
Arabidopsis thaliana
NCBI taxonomy Id: 3702
Other names: A. thaliana, Arabidopsis thaliana (L.) Heynh., mouse-ear cress, thale cress, thale-cress
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