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
AMAG_02249DNA-(apurinic or apyrimidinic site) lyase; Belongs to the DNA repair enzymes AP/ExoA family. (569 aa)    
Predicted Functional Partners:
AMAG_06207
Apurinic endonuclease (APN1).
   
 0.981
AMAG_11728
Apurinic endonuclease (APN1).
   
 0.981
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; Belongs to the Nth/MutY family.
  
 0.891
NTH1-2
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.
  
 0.891
AMAG_03571
Small nuclear ribonucleoprotein G.
   
 0.862
AMAG_10257
Exodeoxyribonuclease III (Xth).
  
  
  0.855
AMAG_00415
Small nuclear ribonucleoprotein Sm D3.
   
 0.850
AMAG_01936
Small nuclear ribonucleoprotein Sm D3.
   
 0.850
FEN1
Flap endonuclease 1; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site- terminated flap. Acts as [...]
  
 0.843
FEN1-2
Flap endonuclease 1; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site- terminated flap. Acts as [...]
  
 0.843
Your Current Organism:
Allomyces macrogynus
NCBI taxonomy Id: 578462
Other names: A. macrogynus ATCC 38327, Allomyces macrogynus ATCC 38327
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.