ILS1/YBL076C Summary Help

Standard Name ILS1 1
Systematic Name YBL076C
Feature Type ORF, Verified
Description Cytoplasmic isoleucine-tRNA synthetase; target of the G1-specific inhibitor reveromycin A (2, 3, 4 and see Summary Paragraph)
Name Description IsoLeucine-tRNA Synthetase
Chromosomal Location
ChrII:84261 to 81043 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -43 cM
Gene Ontology Annotations All ILS1 GO evidence and references
  View Computational GO annotations for ILS1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 8 genes
Large-scale survey
reduction of function
48 total interaction(s) for 38 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 34
  • Affinity Capture-RNA: 4
  • PCA: 1

Genetic Interactions
  • Negative Genetic: 7
  • Positive Genetic: 1
  • Synthetic Lethality: 1

Expression Summary
Length (a.a.) 1,072
Molecular Weight (Da) 122,982
Isoelectric Point (pI) 5.94
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrII:84261 to 81043 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Genetic position: -43 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..3219 84261..81043 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000172

About aminoacyl-tRNA synthetases...

In a process critical for accurate translation of the genetic code, aminoacyl-tRNA synthetases (aka aminoacyl-tRNA ligases) attach amino acids specifically to cognate tRNAs, thereby "charging" the tRNAs. The catalysis is accomplished via a two-step mechanism. First, the synthetase activates the amino acid in an ATP-dependent reaction, producing aminoacyl-adenylate and releasing inorganic pyrophosphate (PPi). Second, the enzyme binds the correct tRNA and transfers the activated amino acid to either the 2' or 3' terminal hydroxyl group of the tRNA, forming the aminoacyl-tRNA and AMP (5, 6 and references therein).

Aminoacyl-tRNA synthetases possess precise substrate specificity and, despite their similarity in function, vary in size, primary sequence and subunit composition. Individual members of the aminoacyl-tRNA synthetase family can be categorized in one of two classes, depending on amino acid specificity. Class I enzymes (those specific for Glu, Gln, Arg, Cys, Met, Val, Ile, Leu, Tyr and Trp) typically contain two highly conserved sequence motifs, are monomeric or dimeric, and aminoacylate at the 2' terminal hydroxyl of the appropriate tRNA. Class II enzymes (those specific for Gly, Ala, Pro, Ser, Thr, His, Asp, Asn, Lys and Phe) typically contain three highly conserved sequence motifs, are dimeric or tetrameric, and aminoacylate at the 3' terminal hydroxyl of the appropriate tRNA (5, 6, 7 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for ILS1
1) Nelbock, P., et al.  (1989) ; Personal Communication, Mortimer Map Edition 10
2) Englisch U, et al.  (1987) Structure of the yeast isoleucyl-tRNA synthetase gene (ILS1). DNA-sequence, amino-acid sequence of proteolytic peptides of the enzyme and comparison of the structure to those of other known aminoacyl-tRNA synthetases. Biol Chem Hoppe Seyler 368(8):971-9
3) Meussdoerffer F and Fink GR  (1983) Structure and expression of two aminoacyl-tRNA synthetase genes from Saccharomyces cerevisiae. J Biol Chem 258(10):6293-9
4) Miyamoto Y, et al.  (2002) Identification of Saccharomyces cerevisiae isoleucyl-tRNA synthetase as a target of the G1-specific inhibitor Reveromycin A. J Biol Chem 277(32):28810-4
5) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
6) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
7) Eriani G, et al.  (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347(6289):203-6