STRINGSTRING
METTL24 METTL24 RRNAD1 RRNAD1 METTL25 METTL25 EEF1AKMT2 EEF1AKMT2 AS3MT AS3MT MEPCE MEPCE GSTCD GSTCD
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:
METTL24Methyltransferase-like protein 24; Methyltransferase like 24. (366 aa)
RRNAD1Protein RRNAD1; Ribosomal RNA adenine dimethylase domain containing 1; Belongs to the RRNAD1 family. (475 aa)
METTL25Methyltransferase-like protein 25; Putative methyltransferase. (603 aa)
EEF1AKMT2EEF1A 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. (291 aa)
AS3MTArsenite methyltransferase; Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH. (375 aa)
MEPCE7SK snRNA methylphosphate capping enzyme; S-adenosyl-L-methionine-dependent methyltransferase that adds a methylphosphate cap at the 5'-end of 7SK snRNA, leading to stabilize it. (689 aa)
GSTCDGlutathione S-transferase C-terminal domain containing; Belongs to the GSTCD family. (633 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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