WARS (gene)

Tryptophanyl-tRNA synthetase
File:PBB Protein WARS image.jpg PDB rendering based on 1o5t.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1o5t​, 1r6t​, 1r6u​, 1ulh​, 2ake​, 2azx​, 2dr2​
Identifiers
Symbols	WARS ; GAMMA-2; IFI53; IFP53
External IDs	Template:OMIM5 Template:MGI HomoloGene: 3084
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE WARS 200629 at tn.png
File:PBB GE WARS 200628 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Tryptophanyl-tRNA synthetase, also known as WARS, is a human gene.

Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Two forms of tryptophanyl-tRNA synthetase exist, a cytoplasmic form, named WARS, and a mitochondrial form, named WARS2. Tryptophanyl-tRNA synthetase (WARS) catalyzes the aminoacylation of tRNA(trp) with tryptophan and is induced by interferon. Tryptophanyl-tRNA synthetase belongs to the class I tRNA synthetase family. Four transcript variants encoding two different isoforms have been found for this gene.

Further reading

• Ewalt KL, Schimmel P (2002). "Activation of angiogenic signaling pathways by two human tRNA synthetases". Biochemistry. 41 (45): 13344–9. PMID 12416978.
• Rasmussen HH, van Damme J, Puype M; et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. PMID 1286667.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bange FC, Flohr T, Buwitt U, Böttger EC (1992). "An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase". FEBS Lett. 300 (2): 162–6. PMID 1373391.CS1 maint: Multiple names: authors list (link)
• Buwitt U, Flohr T, Böttger EC (1992). "Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor". EMBO J. 11 (2): 489–96. PMID 1537332.CS1 maint: Multiple names: authors list (link)
• Rubin BY, Anderson SL, Xing L; et al. (1992). "Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts". J. Biol. Chem. 266 (36): 24245–8. PMID 1761529.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fleckner J, Rasmussen HH, Justesen J (1992). "Human interferon gamma potently induces the synthesis of a 55-kDa protein (gamma 2) highly homologous to rabbit peptide chain release factor and bovine tryptophanyl-tRNA synthetase". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11520–4. PMID 1763065.CS1 maint: Multiple names: authors list (link)
• Frolova LYu , Sudomoina MA, Grigorieva AYu; et al. (1992). "Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase". Gene. 109 (2): 291–6. PMID 1765274.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL (1993). "The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization". Gene. 128 (2): 237–45. PMID 7685728.CS1 maint: Multiple names: authors list (link)
• Popenko VI, Cherny NE, Beresten SF; et al. (1994). "Immunoelectron microscopic location of tryptophanyl-tRNA synthetase in mammalian, prokaryotic and archaebacterial cells". Eur. J. Cell Biol. 62 (2): 248–58. PMID 7925483.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Børglum AD, Flint T, Tommerup N; et al. (1996). "Assignment of the human tryptophanyl-tRNA synthetase gene (WARS) to chromosome 14q32.2 --> q32.32". Cytogenet. Cell Genet. 73 (1–2): 99–103. PMID 8646895.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sokolova IV, Narovlianskiĭ AN, Amchenkova AM, Turpaev KT (1996). "[Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene]". Mol. Biol. (Mosk.). 30 (2): 319–29. PMID 8724762.CS1 maint: Multiple names: authors list (link)
• Krause SW, Rehli M, Kreutz M; et al. (1996). "Differential screening identifies genetic markers of monocyte to macrophage maturation". J. Leukoc. Biol. 60 (4): 540–5. PMID 8864140.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yuan W, Collado-Hidalgo A, Yufit T; et al. (1998). "Modulation of cellular tryptophan metabolism in human fibroblasts by transforming growth factor-beta: selective inhibition of indoleamine 2,3-dioxygenase and tryptophanyl-tRNA synthetase gene expression". J. Cell. Physiol. 177 (1): 174–86. doi:10.1002/(SICI)1097-4652(199810)177:1<174::AID-JCP18>3.0.CO;2-D. PMID 9731757.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jensen LL, Nielsen MM, Justesen J, Hansen LL (2001). "Assignment of human NADH dehydrogenase (ubiquinone) 1 beta subcomplex 3 (NDUFB3) and of its four pseudogenes to human chromosomes 2q31.3, 1p13.3-->p13.1, 9q32-->q34.1, 14q22.3-->q23.1 and 14q32.2 by radiation hybrid mapping". Cytogenet. Cell Genet. 93 (1–2): 147–50. PMID 11474204.CS1 maint: Multiple names: authors list (link)
• Otani A, Slike BM, Dorrell MI; et al. (2002). "A fragment of human TrpRS as a potent antagonist of ocular angiogenesis". Proc. Natl. Acad. Sci. U.S.A. 99 (1): 178–83. doi:10.1073/pnas.012601899. PMID 11773625.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wakasugi K, Slike BM, Hood J; et al. (2002). "A human aminoacyl-tRNA synthetase as a regulator of angiogenesis". Proc. Natl. Acad. Sci. U.S.A. 99 (1): 173–7. doi:10.1073/pnas.012602099. PMID 11773626.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sang Lee J, Gyu Park S, Park H; et al. (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID 11829477.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Guo Q, Gong Q, Tong KL; et al. (2002). "Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains". J. Biol. Chem. 277 (16): 14343–9. doi:10.1074/jbc.M111745200. PMID 11834741.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)