GLN4/YOR168W Summary Help

Standard Name GLN4 1
Systematic Name YOR168W
Feature Type ORF, Verified
Description Glutamine tRNA synthetase; monomeric class I tRNA synthetase that catalyzes the specific glutaminylation of tRNA(Gln); N-terminal domain proposed to be involved in enzyme-tRNA interactions (1, 2, 3 and see Summary Paragraph)
Name Description GLutamiNe metabolism 1
Gene Product Alias glutaminyl-tRNA synthetase
Chromosomal Location
ChrXV:649303 to 651732 | ORF Map | GBrowse
Genetic position: 88 cM
Gene Ontology Annotations All GLN4 GO evidence and references
  View Computational GO annotations for GLN4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 3 genes
Classical genetics
reduction of function
Large-scale survey
reduction of function
22 total interaction(s) for 19 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 12
  • Affinity Capture-RNA: 3
  • Biochemical Activity: 2
  • Reconstituted Complex: 1

Genetic Interactions
  • Synthetic Lethality: 4

Expression Summary
Length (a.a.) 809
Molecular Weight (Da) 93,132
Isoelectric Point (pI) 8.7
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXV:649303 to 651732 | ORF Map | GBrowse
Genetic position: 88 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2430 649303..651732 2011-02-03 1996-07-31
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 SGDIDS000005694

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 (4, 5 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 (4, 5, 6 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for GLN4
1) Ludmerer SW and Schimmel P  (1985) Cloning of GLN4: an essential gene that encodes glutaminyl-tRNA synthetase in Saccharomyces cerevisiae. J Bacteriol 163(2):763-8
2) Ludmerer SW, et al.  (1993) Purification of glutamine tRNA synthetase from Saccharomyces cerevisiae. A monomeric aminoacyl-tRNA synthetase with a large and dispensable NH2-terminal domain. J Biol Chem 268(8):5519-23
3) Whelihan EF and Schimmel P  (1997) Rescuing an essential enzyme-RNA complex with a non-essential appended domain. EMBO J 16(10):2968-74
4) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
5) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
6) 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