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.
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
NPVFPro-FMRFamide-related neuropeptide VF. (173 aa)    
Predicted Functional Partners:
NPFFR1
Neuropeptide FF receptor 1.
     
 0.988
UQCRFS1
Cytochrome b-c1 complex subunit Rieske, mitochondrial.
  
 0.930
UQCRB
Ubiquinol-cytochrome c reductase subunit 7.
   
 0.910
UQCRQ
Ubiquinol-cytochrome c reductase subunit 8.
   
 0.905
UQCR10
Ubiquinol-cytochrome c reductase subunit 9.
   
 0.900
COX4I1
Cytochrome c oxidase subunit 4 isoform 1, mitochondrial isoform X1.
   
 0.884
APAF1
Apoptotic protease-activating factor 1 isoform X1.
   
 0.869
LOC107208290
Cytochrome b-c1 complex subunit 6, mitochondrial.
   
 0.862
UQCRC2
Cytochrome b-c1 complex subunit 2, mitochondrial.
   
 0.829
COX1
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.
  
 0.802
Your Current Organism:
Parus major
NCBI taxonomy Id: 9157
Other names: Great Tit, Kohlmeise, P. major
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