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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
TSR3TSR3, acp transferase ribosome maturation factor; Ribosome biogenesis protein TSR3 homolog; Probable pre-rRNA processing protein involved in ribosome biogenesis (312 aa)    
Predicted Functional Partners:
TSR2
Pre-rRNA-processing protein TSR2 homolog; May be involved in 20S pre-rRNA processing
   
  
 0.879
TRMT12
tRNA wybutosine-synthesizing protein 2 homolog; S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha- carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86; Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM5/TYW2 family
   
  
 0.773
TSR1
Pre-rRNA-processing protein TSR1 homolog; Required during maturation of the 40S ribosomal subunit in the nucleolus
   
  
 0.766
NOB1
RNA-binding protein NOB1; May play a role in mRNA degradation; Belongs to the NOB1 family
   
  
 0.765
RRP8
Ribosomal RNA-processing protein 8; Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys- 9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and pr [...]
   
 
 0.757
CFP
Complement factor properdin; Properdin; A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes
      
 0.754
ADAMTSL2
ADAMTS-like protein 2; ADAMTS like 2
      
 0.745
EMG1
Ribosomal RNA small subunit methyltransferase NEP1; S-adenosyl-L-methionine-dependent pseudouridine N(1)- methyltransferase that methylates pseudouridine at position 1248 (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-riboso [...]
   
  
 0.724
OPLAH
5-oxoprolinase (ATP-hydrolysing); 5-oxoprolinase; Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate
 
 
    0.723
TBL2
Transducin beta-like protein 2; WD repeat domain containing
     
 0.722
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.