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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
C12orf65Probable peptide chain release factor C12orf65, mitochondrial; May act as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion. May help rescuing stalled mitoribosomes during translation (By similarity) (166 aa)    
Predicted Functional Partners:
ICT1
Peptidyl-tRNA hydrolase ICT1, mitochondrial; Essential peptidyl-tRNA hydrolase component of the mitochondrial large ribosomal subunit. Acts as a codon-independent translation release factor that has lost all stop codon specificity and directs the termination of translation in mitochondrion, possibly in case of abortive elongation. May be involved in the hydrolysis of peptidyl-tRNAs that have been prematurely terminated and thus in the recycling of stalled mitochondrial ribosomes
   
 
 0.939
MRPS16
Mitochondrial ribosomal protein S16; Belongs to the bacterial ribosomal protein bS16 family
  
 
 0.937
GFM1
Elongation factor G, mitochondrial; Mitochondrial GTPase that catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A- site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mit [...]
  
  
 0.841
TSFM
Elongation factor Ts, mitochondrial; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome; Belongs to the EF-Ts family
  
  
 0.822
TUFM
Elongation factor Tu, mitochondrial; This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily
   
 
 0.816
HOGA1
4-hydroxy-2-oxoglutarate aldolase, mitochondrial; Catalyzes the final step in the metabolic pathway of hydroxyproline
   
  
 0.811
MTRF1L
Peptide chain release factor 1-like, mitochondrial; Mitochondrial peptide chain release factor that directs the termination of translation in response to the peptide chain termination codons UAA and UAG
   
  
 0.801
MRPL17
Mitochondrial ribosomal protein L17
  
 
 0.770
MRPS22
Mitochondrial ribosomal protein S22; Belongs to the mitochondrion-specific ribosomal protein mS22 family
   
  
 0.751
MRRF
Ribosome-recycling factor, mitochondrial; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another (By similarity)
  
  
 0.747
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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