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
B0A48_00817Uncharacterized protein. (725 aa)    
Predicted Functional Partners:
B0A48_14808
CID domain-containing protein.
   
 
 0.853
B0A48_14146
CID domain-containing protein.
   
 
 0.853
B0A48_13972
Sister chromatid cohesion protein.
   
    0.653
B0A48_15857
Nuclear cap-binding protein subunit 2.
    
 
 0.539
B0A48_17516
Uncharacterized protein.
   
  0.513
B0A48_07803
Uncharacterized protein.
   
  0.513
NTH1
Endonuclease III homolog; Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
   
 
 0.474
B0A48_00005
5'-3' exoribonuclease; Possesses 5'->3' exoribonuclease activity. May promote termination of transcription by RNA polymerase II.
   
 
 0.474
B0A48_18474
Transcription elongation factor SPT5; The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene.
    
 
 0.468
B0A48_18606
Transcription elongation factor SPT5; The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene.
    
 
 0.468
Your Current Organism:
Rachicladosporium antarcticum
NCBI taxonomy Id: 1507870
Other names: CCFEE 5527, R. antarcticum, Rachicladosporium antarcticum Onofri & Egidi, 2014
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