STRINGSTRING
AHC39228.1 AHC39228.1 nuoK nuoK AHC38960.1 AHC38960.1 AHC39264.1 AHC39264.1 nuoC nuoC AHC39427.1 AHC39427.1 AHC38889.1 AHC38889.1 nuoI nuoI nuoB nuoB AHC39444.1 AHC39444.1
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:
AHC39228.1NADH dehydrogenase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. (181 aa)
nuoKNADH-quinone oxidoreductase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I subunit 4L family. (108 aa)
AHC38960.1NADH:ubiquinone oxidoreductase 17.2 kD subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (97 aa)
AHC39264.1NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (420 aa)
nuoCNADH-quinone oxidoreductase subunit C; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. (192 aa)
AHC39427.12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (171 aa)
AHC38889.1NADH-ubiquinone oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (320 aa)
nuoINADH dehydrogenase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (169 aa)
nuoBNADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. (177 aa)
AHC39444.1Cation:proton antiporter; Derived by automated computational analysis using gene prediction method: Protein Homology. (494 aa)
Your Current Organism:
Ehrlichia muris
NCBI taxonomy Id: 1423892
Other names: E. muris AS145, Ehrlichia muris AS145
Server load: low (22%) [HD]