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
METTL22Methyltransferase-like protein 22; Protein N-lysine methyltransferase. In vitro methylates KIN; Belongs to the methyltransferase superfamily. METTL22 family (404 aa)    
Predicted Functional Partners:
KIN
DNA/RNA-binding protein KIN17; Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro; Belongs to the KIN17 family
   
 0.993
METTL18
Histidine protein methyltransferase 1 homolog; Probable histidine methyltransferase
   
  
 0.797
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
    
 
 0.783
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
    
 
 0.771
FAM86A
Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'
      
 0.766
METTL20
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
   
  
 0.753
METTL23
Methyltransferase-like protein 23; Probable methyltransferase
    
 
 0.747
HRSP12
2-iminobutanoate/2-iminopropanoate deaminase; Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase
      
 0.729
TMEM186
Transmembrane protein 186
      
 0.670
N6AMT2
EEF1A lysine methyltransferase 1; Protein-lysine methyltransferase that selectively catalyzes the trimethylation of EEF1A at 'Lys-79'
   
  
 0.656
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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