STRINGSTRING
MST1 MST1 NAM2 NAM2 ALA1 ALA1 CDC60 CDC60 RPS23B RPS23B MES1 MES1 MSM1 MSM1 RPS23A RPS23A AIM10 AIM10 YHR020W YHR020W THS1 THS1
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.
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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:
MST1Threonine--tRNA ligase, mitochondrial; Mitochondrial threonyl-tRNA synthetase; aminoacylates both the canonical threonine tRNA tT(UGU)Q1 and the unusual threonine tRNA tT(UAG)Q2 in vitro; lacks a typical editing domain, but has pre-transfer editing activity stimulated by the unusual tRNA-Thr. (462 aa)
NAM2Leucine--tRNA ligase, mitochondrial; Mitochondrial leucyl-tRNA synthetase; also has direct role in splicing of several mitochondrial group I introns; indirectly required for mitochondrial genome maintenance; human homolog LARS2 can complement yeast null mutant, and is implicated in Perrault syndrome; Belongs to the class-I aminoacyl-tRNA synthetase family. (894 aa)
ALA1Alanine--tRNA ligase, mitochondrial; Cytoplasmic and mitochondrial alanyl-tRNA synthetase; required for protein synthesis; point mutation (cdc64-1 allele) causes cell cycle arrest at G1; lethality of null mutation is functionally complemented by human homolog AARS; mutations in human homolog AARS are associated with autoimmune disease polymyositis/dermatomyositis; Belongs to the class-II aminoacyl-tRNA synthetase family. (958 aa)
CDC60Leucine--tRNA ligase, cytoplasmic; Cytosolic leucyl tRNA synthetase; ligates leucine to the appropriate tRNA; human homolog LARS can complement yeast temperature-sensitive mutant at restrictive temperature. (1090 aa)
RPS23BRibosomal protein 28 (rp28) of the small (40S) ribosomal subunit; required for translational accuracy; homologous to mammalian ribosomal protein S23 and bacterial S12; RPS23B has a paralog, RPS23A, that arose from the whole genome duplication; deletion of both RPS23A and RPS23B is lethal. (145 aa)
MES1Methionine--tRNA ligase, cytoplasmic; 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; mutations in human ortholog MARS are associated with pediatric pulmonary alveolar proteinosis. (751 aa)
MSM1Methionine--tRNA ligase, mitochondrial; 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)
RPS23ARibosomal protein 28 (rp28) of the small (40S) ribosomal subunit; required for translational accuracy; homologous to mammalian ribosomal protein S23 and bacterial S12; RPS23A has a paralog, RPS23B, that arose from the whole genome duplication; deletion of both RPS23A and RPS23B is lethal. (145 aa)
AIM10Probable proline--tRNA ligase, mitochondrial; 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)
YHR020WPutative proline--tRNA ligase YHR020W; Prolyl-tRNA synthetase; N-terminal domain shows weak homology to prokaryotic posttransfer editing domain, but does not possess posttransfer editing activity; may interact with ribosomes, based on co-purification experiments. (688 aa)
THS1Threonine--tRNA ligase, cytoplasmic; Threonyl-tRNA synthetase; essential cytoplasmic protein; human homolog TARS can complement yeast null mutant. (734 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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