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The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
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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
rpoKDNA-directed RNA polymerase, subunit K/omega; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoK/eukaryotic RPB6 RNA polymerase subunit family. (61 aa)    
Predicted Functional Partners:
rpoN
DNA-directed RNA polymerase, subunit N (RpoN/RPB10); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoN/eukaryotic RPB10 RNA polymerase subunit family.
 
 0.999
rpoD
DNA-directed RNA polymerase, alpha subunit/40 kD subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoD/eukaryotic RPB3 RNA polymerase subunit family.
  
 0.998
rpoH
DNA-directed RNA polymerase, subunit H, RpoH/RPB5; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoH/eukaryotic RPB5 RNA polymerase subunit family.
  
 0.997
rpoP
DNA-directed RNA polymerase, subunit RPC10 (contains C4-type Zn-finger); DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoP/eukaryotic RPC10 RNA polymerase subunit family.
   
 0.991
rpoL
DNA-directed RNA polymerase, subunit L; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Belongs to the archaeal RpoL/eukaryotic RPB11/RPC19 RNA polymerase subunit family.
   
 0.990
rps2
PFAM: Ribosomal protein S2; TIGRFAM: ribosomal protein Sa(cytosolic)/S2(archaeal); Belongs to the universal ribosomal protein uS2 family.
  
 
 0.988
AGB15101.1
DNA-directed RNA polymerase subunit A'; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 0.984
rpoA2
DNA-directed RNA polymerase, subunit A'; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 0.982
AGB17127.1
PFAM: S1 RNA binding domain; RNA polymerase Rpb7-like, N-terminal domain; TIGRFAM: DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form.
   
 0.982
AGB15100.1
DNA-directed RNA polymerase subunit B; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
 
 0.976
Your Current Organism:
Halovivax ruber
NCBI taxonomy Id: 797302
Other names: H. ruber XH-70, Halovivax ruber JCM 13892, Halovivax ruber XH-70, Halovivax ruber str. XH-70, Halovivax ruber strain XH-70
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