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HTS1 protein (Saccharomyces cerevisiae) - STRING interaction network
"HTS1" - Cytoplasmic and mitochondrial histidine tRNA synthetase in Saccharomyces cerevisiae
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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HTS1Cytoplasmic and mitochondrial histidine tRNA synthetase; efficient mitochondrial localization requires both a presequence and an amino-terminal sequence; mutations in human ortholog HARS2 are associated with Perrault syndrome; Catalyzes the aminoacylation of histidyl-tRNA in both the cytoplasm and the mitochondrion (546 aa)    
Predicted Functional Partners:
THS1
Threonyl-tRNA synthetase, essential cytoplasmic protein (734 aa)
   
 
  0.960
GRS1
Cytoplasmic and mitochondrial glycyl-tRNA synthase that ligates glycine to the cognate anticodon bearing tRNA; transcription termination factor that may interact with the 3’-end of pre-mRNA to promote 3’-end formation; Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs (By similarity) (667 aa)
     
 
  0.953
MSF1
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)
   
   
  0.949
HIS4
Multifunctional enzyme containing phosphoribosyl-ATP pyrophosphatase, phosphoribosyl-AMP cyclohydrolase, and histidinol dehydrogenase activities; catalyzes the second, third, ninth and tenth steps in histidine biosynthesis (799 aa)
       
  0.939
KRS1
Lysyl-tRNA synthetase (591 aa)
     
   
  0.938
SES1
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)
   
 
  0.925
VAS1
Mitochondrial and cytoplasmic valyl-tRNA synthetase (1104 aa)
   
   
  0.912
TYS1
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)
   
   
  0.905
GCN1
Positive regulator of the Gcn2p kinase activity, forms a complex with Gcn20p; proposed to stimulate Gcn2p activation by an uncharged tRNA; Acts as a positive activator of the GCN2 protein kinase activity in response to amino acid starvation (PubMed-8497269, PubMed-24333428). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN1 seems to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA- binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed-7621 [...] (2672 aa)
     
 
  0.903
CDC60
Cytosolic leucyl tRNA synthetase, ligates leucine to the appropriate tRNA (1090 aa)
   
   
  0.901
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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