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
tfb-3Transcription initiation factor TFB; Stabilizes TBP binding to an archaeal box-A promoter. Also responsible for recruiting RNA polymerase II to the pre-initiation complex (DNA-TBP-TFIIB). (305 aa)    
Predicted Functional Partners:
tbp-2
Transcription factor; General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
  
 0.960
tbp
Transcription factor; General factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Binds specifically to the TATA box promoter element which lies close to the position of transcription initiation.
  
 0.959
C448_01444
Transcription factor; COG2101 TATA-box binding protein (TBP), component of TFIID and TFIIIB.
  
 0.957
rpoK
DNA-directed RNA polymerase subunit K; 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.
  
 
 0.812
rpoH
DNA-directed RNA polymerase subunit H; 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.
  
 
 0.805
rpoD
DNA-directed RNA polymerase subunit D; 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.
  
 
 0.802
tfe
Transcription factor TFIIE subunit alpha; Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation [...]
    
 0.799
C448_11211
COG1594 DNA-directed RNA polymerase, subunit M/Transcription elongation factor TFIIS; Belongs to the archaeal rpoM/eukaryotic RPA12/RPB9/RPC11 RNA polymerase family.
  
 
 0.788
rpoN
DNA-directed RNA polymerase subunit N; 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.
  
 
 0.778
C448_02321
COG0085 DNA-directed RNA polymerase, beta subunit/140 kD subunit; Belongs to the RNA polymerase beta chain family.
  
 
 0.769
Your Current Organism:
Halococcus morrhuae
NCBI taxonomy Id: 931277
Other names: H. morrhuae DSM 1307, Halococcus morrhuae DSM 1307, Halococcus morrhuae JCM 8876, Halococcus morrhuae NRC 16008
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.