STRING allows inspection of the interaction evidence for any given network. Choose any of the viewers above (disabled if not applicable in your network).
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.
colored nodes: query proteins and first shell of interactors
white nodes: second shell of interactors
empty nodes: proteins of unknown 3D structure
filled nodes: some 3D structure is known or predicted
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.
from curated databases
Uncharacterized protein y4iJ; y4iJ; NGR234_159 (596 aa)
Predicted Functional Partners:
Uncharacterized protein y4iI; y4iI; NGR234_158 (703 aa)
Uncharacterized protein y4iK; y4iK; NGR234_160 (232 aa)
Uncharacterized protein y4iL; y4iL; NGR234_161 (432 aa)
annotation not available (302 aa)
annotation not available (368 aa)
Uncharacterized protein y4iM; y4iM; NGR234_162 (432 aa)
annotation not available (448 aa)
Periplasmic nitrate reductase; Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism (843 aa)
annotation not available (710 aa)
Cytochrome c oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (593 aa)