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
laf-1ATP-dependent RNA helicase laf-1; Multifunctional ATP-dependent RNA helicase. Plays a role in RNA remodeling, but is not required for RNA unwinding. Binds to RNA in a concentration-dependent manner to stimulate annealing between two complementary strands of RNA. This process is also dependent upon ATP; ATP reduces binding to RNA and subsequently diminishes RNA annealing. Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in the regulation of transcription and translation initiation. Involved in innate immunity (By si [...] (708 aa)    
Predicted Functional Partners:
hrp-1
Heterogeneous nuclear ribonucleoprotein A1; This protein is a component of ribonucleosomes. Overexpression gradually increases telomere length, leading to increase lifespan.
 
 
 
 0.852
meg-3
Uncharacterized protein.
    
 
 0.748
ccdc-47
CCDC (Human Coiled Coil Domain Containing) homolog.
      
 0.697
tra-2
Sex-determining transformer protein 2; Plays a major role in controlling sexual cell fates. Promotes female development in XX animals where it sequesters one or more of the FEM proteins to the membrane thereby freeing the tra-1 protein (a putative transcription factor) to enter the nucleus and promote female development. In XO animals it acts as a receptor for her-1 which prevents it from binding to FEM proteins thereby repressing the activity of tra-1. Negatively regulates male development when bound to fem-3 and is required together with tra-1 for promoting spermatogenesis. Also requ [...]
      
 0.696
atp-3
ATP synthase subunit.
  
 
 0.691
eftu-2
Tr-type G domain-containing protein.
   
 
 0.691
pgl-1
Guanyl-specific ribonuclease pgl-1; Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate. Together with the P-granule component pgl-3, is involved in the formation of P-granules. Together with pgl-3, probably recruits other granule components such as pos-1, mex-3 and glh-1 to P-granules. In addition, may act redundantly with pgl-3 to protect germ cells from excessive germline apoptosis du [...]
  
 
 0.681
atp-5
ATP synthase subunit.
   
   0.661
prp-6
Yeast PRP (Splicing factor) related.
   
 
 0.660
atp-2
ATP synthase subunit beta, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the c [...]
  
 
 0.659
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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