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STRINGSTRING
PRO4 protein (Zea mays) - STRING interaction network
"PRO4" - Profilin-4 in Zea mays
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
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Gene Fusion
Cooccurence
Coexpression
Experiments
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[Homology]
Score
PRO4Profilin-4; Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Has a high affinity for poly-proline (131 aa)    
Predicted Functional Partners:
CYP
Peptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family (172 aa)
     
   
  0.842
GRMZM2G157018_P01
ATP synthase subunit d, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the cent [...] (170 aa)
     
   
  0.838
PRO5
Profilin-5; Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Has a high affinity for poly-proline (131 aa)
     
   
0.832
eno1
Enolase 1 (446 aa)
     
 
  0.830
pco095216b
Actin-7; Putative actin family protein isoform 1; Putative actin family protein isoform 2; Putative actin family protein isoform 3; Uncharacterized protein ; Belongs to the actin family (377 aa)
     
 
  0.806
umc2243
Actin-7; Belongs to the actin family (377 aa)
       
 
  0.769
100304239
Actin-7; Belongs to the actin family (377 aa)
       
 
  0.769
103625937
Actin-1 ; Belongs to the actin family (377 aa)
       
 
  0.754
GRMZM2G067985_P05
Actin-7; Actin-97; Putative actin family protein isoform 1; Putative actin family protein isoform 2; Putative actin family protein isoform 3; Putative actin family protein isoform 4; Uncharacterized protein ; Belongs to the actin family (430 aa)
     
 
  0.739
GRMZM2G110378_P04
Actin-97; Putative actin family protein isoform 1; Putative actin family protein isoform 2; Putative actin family protein isoform 3; Putative actin family protein isoform 4; Uncharacterized protein ; Belongs to the actin family (377 aa)
     
 
  0.728
Your Current Organism:
Zea mays
NCBI taxonomy Id: 4577
Other names: Z. mays, Zea mays, Zea mays L., Zea mays var. japonica, maize
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