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
parp-2Poly [ADP-ribose] polymerase 2; Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation, a post-translational modification synthesized after DNA damage that appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks and programmed cell death. (538 aa)    
Predicted Functional Partners:
parp-1
Poly [ADP-ribose] polymerase 1; Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation, a post-translational modification synthesized after DNA damage that appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks and programmed cell death. Involved in protection of the genome against mutations.
  
 
0.945
parg-2
Poly(ADP-ribose) glycohydrolase 2; Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells (By similarity).
    
 
 0.942
parg-1
Poly(ADP-ribose) glycohydrolase 1; Poly(ADP-ribose) synthesized after DNA damage is only present transiently and is rapidly degraded by poly(ADP-ribose) glycohydrolase. Poly(ADP-ribose) metabolism may be required for maintenance of the normal function of neuronal cells (By similarity).
   
 
 0.884
F52C12.1
Probable tyrosyl-DNA phosphodiesterase; DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead- end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. May have low 3'exonuclease activity and may be able to remove a sin [...]
   
 
 0.860
crn-1
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 [...]
   
 
 0.811
JC8.7
Uncharacterized protein.
   
 
 0.805
cku-70
Ku domain-containing protein.
   
 
 0.774
lig-4
LIGase.
   
 
 0.735
ung-1
Uracil-DNA glycosylase; Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
   
  
 0.726
lig-1
DNA ligase 1; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
   
 
 0.711
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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