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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
atpEF0F1 ATP synthase subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 central stalk subunits to proton translocation. (75 aa)    
Predicted Functional Partners:
atpD
ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
  
 0.999
atpA
ATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
  
 0.999
atpB
F-ATPase subunit 6; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family.
 
 0.998
atpC
F-ATPase epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane.
  
 0.996
atpF_2
F-type ATPase subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
 
 
 0.995
atpG
F-ATPase gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
  
 0.994
atpH
F-type ATPase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 central stalk subunits to proton translocation.
  
 0.994
atpF_1
F-type ATPase subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
 
 
 0.993
BV96_04229
Transmembrane protein EpsH.
  
 0.988
rpsN
30S ribosomal protein S14; Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site; Belongs to the universal ribosomal protein uS14 family.
  
  
 0.898
Your Current Organism:
Sphingomonas paucimobilis
NCBI taxonomy Id: 13689
Other names: ATCC 10829 [[Flavobacterium devorans]], ATCC 29837, Bacillus devorans, CCUG 31192, CCUG 6518, CIP 100752, Chromobacterium devorans, DSM 30198 [[Flavobacterium devorans]], Flavobacterium devorans, GIFU 2395, GIFU:2395, IFO 13935, JCM 7516, LMG 4017 [[Flavobacterium devorans]], LMG:4017 [[Flavobacterium devorans]], NBRC 13935, NCAIM B.01654, NCPPB 3838, NCTC 11030, NRRL B-54 [[Flavobacterium devorans]], Pseudomonas paucimobilis, S. paucimobilis
Server load: medium (54%) [HD]