NAM2 protein (Saccharomyces cerevisiae) - STRING interaction network
"NAM2" - Mitochondrial leucyl-tRNA synthetase, also has a direct role in splicing of several mitochondrial group I introns in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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Gene Fusion
NAM2Mitochondrial leucyl-tRNA synthetase, also has a direct role in splicing of several mitochondrial group I introns; indirectly required for mitochondrial genome maintenance (894 aa)    
Predicted Functional Partners:
Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss (576 aa)
Protein of unknown function that may interact with ribosomes, based on co-purification experiments; has similarity to proline-tRNA ligase; YHR020W is an essential gene (688 aa)
Cytoplasmic tyrosyl-tRNA synthetase, required for cytoplasmic protein synthesis; interacts with positions 34 and 35 of the tRNATyr anticodon; mutations in human ortholog YARS are associated with Charcot-Marie-Tooth (CMT) neuropathies; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon bases G34, U35 and A36. Also involved in nuclear tRNA [...] (394 aa)
Methionyl-tRNA synthetase, forms a complex with glutamyl-tRNA synthetase (Gus1p) and Arc1p, which increases the catalytic efficiency of both tRNA synthetases; also has a role in nuclear export of tRNAs; Catalyzes the attachment of methionine to tRNA(Met) in a two-step reaction- methionine is first activated by ATP to form Met-AMP and then transferred to the acceptor end of tRNA(Met) (751 aa)
Arginyl-tRNA synthetase, proposed to be cytoplasmic but the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis (607 aa)
Mitochondrial phenylalanyl-tRNA synthetase, active as a monomer, unlike the cytoplasmic subunit which is active as a dimer complexed to a beta subunit dimer; similar to the alpha subunit of E. coli phenylalanyl-tRNA synthetase; Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation (469 aa)
Mitochondrial methionyl-tRNA synthetase (MetRS), functions as a monomer in mitochondrial protein synthesis; functions similarly to cytoplasmic MetRS although the cytoplasmic form contains a zinc-binding domain not found in Msm1p (575 aa)
Glutamyl-tRNA synthetase (GluRS), forms a complex with methionyl-tRNA synthetase (Mes1p) and Arc1p; complex formation increases the catalytic efficiency of both tRNA synthetases and ensures their correct localization to the cytoplasm; Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction- glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). In mitochondria, constitutes the nondiscriminating glutamyl-tRNA synthase that generates the mitochondrial mischarged glutamyl- tRNA(Gln) substrate for the tRNA-dependent amid [...] (708 aa)
Glutamine tRNA synthetase, monomeric class I tRNA synthetase that catalyzes the specific glutaminylation of tRNA(Glu); N-terminal domain proposed to be involved in enzyme-tRNA interactions (809 aa)
Cytosolic seryl-tRNA synthetase, class II aminoacyl-tRNA synthetase that aminoacylates tRNA(Ser), displays tRNA-dependent amino acid recognition which enhances discrimination of the serine substrate, interacts with peroxin Pex21p; Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (462 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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