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
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Co-occurrence
Co-expression
Experiments
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[Homology]
Score
AEB83202.1PFAM: Cytochrome c, class I; KEGG: ajs:Ajs_0710 cytochrome c, class I. (212 aa)    
Predicted Functional Partners:
AEB83274.1
Cytochrome c1; KEGG: ajs:Ajs_0791 cytochrome c1; manually curated; PFAM: Cytochrome c1.
 
 
 0.945
AEB83272.1
Ubiquinol-cytochrome c reductase, iron-sulfur subunit; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 
 0.942
AEB83273.1
Cytochrome b/b6 domain protein; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 
 0.855
AEB82821.1
PFAM: Cytochrome c, class I; KEGG: aav:Aave_0385 cytochrome c, class I.
 
 
 
 0.837
AEB83774.1
PFAM: Cytochrome c, class I; KEGG: dia:Dtpsy_1062 cytochrome c class I.
 
 
 
 0.827
AEB86273.1
Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
 
 
 0.705
AEB83526.1
KEGG: dia:Dtpsy_1001 cbb3-type cytochrome c oxidase subunit II; TIGRFAM: Cytochrome c oxidase, monohaem subunit/FixO; PFAM: Cytochrome c oxidase, monohaem subunit/FixO.
 
 
 0.686
AEB84034.1
PFAM: Cytochrome c oxidase, monohaem subunit/FixO; KEGG: net:Neut_1583 cytochrome c oxidase, mono-heme subunit/FixO.
 
 
 0.681
AEB83525.1
TIGRFAM: Cytochrome c oxidase cbb3-type, subunit I; KEGG: dia:Dtpsy_1000 cbb3-type cytochrome c oxidase subunit I; PFAM: Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family.
 
 
 0.659
AEB84507.1
Gluconate 2-dehydrogenase (acceptor); KEGG: aav:Aave_3387 cytochrome c, class I; PFAM: Cytochrome c, class I.
 
 
 0.658
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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