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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
EEF2KMTProtein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'. (330 aa)    
Predicted Functional Partners:
EEF2
Elongation factor 2; 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.
    
 0.959
EEF1AKMT2
EEF1A lysine methyltransferase 2; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-318'; Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM4 family.
      
 0.806
PRTFDC1
Phosphoribosyltransferase domain-containing protein 1; Has low, barely detectable phosphoribosyltransferase activity (in vitro). Binds GMP, IMP and alpha-D-5-phosphoribosyl 1-pyrophosphate (PRPP). Is not expected to contribute to purine metabolism or GMP salvage; Belongs to the purine/pyrimidine phosphoribosyltransferase family.
    
   0.792
VCPKMT
Protein-lysine methyltransferase METTL21D; Protein-lysine N-methyltransferase that specifically trimethylates 'Lys-315' of VCP/p97; this modification may decrease VCP ATPase activity; Belongs to the methyltransferase superfamily. METTL21 family.
   
 
 0.714
METTL21A
Protein N-lysine methyltransferase METTL21A; Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members. Contributes to the in vivo trimethylation of Lys residues in HSPA1 and HSPA8. In vitro methylates 'Lys-561' in HSPA1, 'Lys-564' in HSPA2, 'Lys-585' in HSPA5, 'Lys-563' in HSPA6 and 'Lys-561' in HSPA8.
   
 
 0.690
ETFBKMT
Electron transfer flavoprotein beta subunit lysine methyltransferase; Protein-lysine methyltransferase that selectively trimethylates the flavoprotein ETFB in mitochondria. Thereby, may negatively regulate the function of ETFB in electron transfer from Acyl-CoA dehydrogenases to the main respiratory chain.
   
 
 0.668
METTL22
Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN. Belongs to the methyltransferase superfamily. METTL22 family.
   
  
 0.648
EEF1AKMT1
EEF1A lysine methyltransferase 1; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'; Belongs to the class I-like SAM-binding methyltransferase superfamily. EFM5 family.
   
  
 0.642
METTL21C
Protein-lysine methyltransferase METTL21C; Protein-lysine methyltransferase. Belongs to the methyltransferase superfamily. METTL21 family.
   
 
 0.641
METTL18
Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase; Belongs to the methyltransferase superfamily. METTL18 family.
   
  
 0.623
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.