STRINGSTRING
STRING protein interaction network
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:
a 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 to 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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
EU95_1999RNA-binding region RNP-1 (RNA recognition motif); Alternative locus ID: PMIT9201_0331. (249 aa)    
Predicted Functional Partners:
gpmI
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate.
   
 0.987
EU95_1141
mRNA 3-end processing factor; Alternative locus ID: PMIT9201_1178.
    
 0.958
EU95_0852
DNA-directed RNA polymerasee alpha subunit; Alternative locus ID: PMIT9201_0675.
    
 0.868
rpoB
DNA-directed RNA polymerasee beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
    
  0.862
ndhJ
NAD(P)H-quinone oxidoreductase chain J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
    
   0.845
EU95_0958
DNA-directed RNA polymerasee omega subunit; Alternative locus ID: PMIT9201_0781.
    
  0.840
ndhH
NAD(P)H-quinone oxidoreductase chain H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
    
   0.840
EU95_1547
High-affnity carbon uptake protein Hat/HatR; Alternative locus ID: PMIT9201_1550.
  
 
 0.823
ndhC
NAD(P)H-quinone oxidoreductase subunit 3; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
    
   0.807
ndhK
NAD(P)H-quinone oxidoreductase chain K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family.
    
   0.807
Your Current Organism:
Prochlorococcus marinus MIT9201
NCBI taxonomy Id: 93057
Other names: P. marinus str. MIT 9201, Prochlorococcus marinus str. MIT 9201, Prochlorococcus sp. MIT 9201, Prochlorococcus sp. MIT9201
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