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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
KVA01_01900Unannotated protein. (122 aa)    
Predicted Functional Partners:
KVA01_06350
Unannotated protein.
  
 0.907
KVA01_17190
Unannotated protein.
   
  0.884
KVA01_17840
Unannotated protein; Belongs to the peptidase M16 family.
   
 0.884
KVA01_17180
Unannotated protein.
   
 0.880
KVA01_21500
Unannotated protein.
   
 0.822
acpP
Unannotated protein; Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family.
   
 0.822
ctaD1
Unannotated protein; 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.
    
  0.787
ctaE
Unannotated protein.
    
  0.781
KVA01_01890
Unannotated protein.
  
    0.775
KVA01_17260
Unannotated protein; 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).
    
  0.744
Your Current Organism:
Kocuria varians
NCBI taxonomy Id: 1272
Other names: ATCC 15306, CCM 884, CCUG 35392, CIP 81.73, DSM 20033, HAMBI 40, IEGM 400, IFO 15358, JCM 7238, K. varians, LMG 14231, LMG:14231, Micrococcus varians, NBRC 15358, NCDO 777, NCTC 7564
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.