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
EKE98396.1KEGG: npu:Npun_R1079 7.7e-193 FAD dependent oxidoreductase; Psort location: Cytoplasmic, score: 9.12. (413 aa)    
Predicted Functional Partners:
EKE98576.1
Hypothetical protein; KEGG: ajs:Ajs_3012 0.010 lipopolysaccharide biosynthesis K08252; Psort location: Periplasmic, score: 9.83.
    
   0.732
EKF02482.1
KEGG: npu:Npun_F0647 2.5e-203 acyl-CoA dehydrogenase type 2.
     
 0.680
EKF01584.1
acyl-CoA dehydrogenase, middle domain protein; KEGG: npu:Npun_R5924 1.2e-132 acyl-CoA dehydrogenase type 2.
     
 0.680
EKE99892.1
KEGG: npu:Npun_F0648 9.9e-97 acyl-CoA dehydrogenase type 2.
     
 0.680
petB
Cytochrome b6; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
    
 
 0.677
EKF01164.1
Hypothetical protein; KEGG: syg:sync_0549 4.1e-20 petB; cytochrome b6 K02635; Psort location: CytoplasmicMembrane, score: 10.00.
    
 
 0.677
EKF05805.1
Cytochrome c oxidase; 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).
    
 
 0.606
EKF04498.1
Cytochrome c oxidase subunit; 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).
    
 
 0.606
EKE98669.1
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).
    
 
 0.606
EKE98779.1
Cytochrome c oxidase subunit; 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).
    
 
 0.606
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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