WARS (gene)

Tryptophanyl-tRNA synthetase

PDB rendering based on 1o5t.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1O5T, 1R6T, 1R6U, 1ULH, 2AKE, 2AZX, 2DR2, 2QUH, 2QUI, 2QUJ, 2QUK

Identifiers

Symbols

WARS ; GAMMA-2; IFI53; IFP53

External IDs

OMIM: 191050 MGI: 104630 HomoloGene: 3084 GeneCards: WARS Gene

EC number

6.1.1.2

Gene ontology
Molecular function	• tryptophan-tRNA ligase activity • protein binding • ATP binding
Cellular component	• nucleus • cytoplasm • cytosol • extracellular exosome
Biological process	• angiogenesis • translation • tRNA aminoacylation for protein translation • tryptophanyl-tRNA aminoacylation • negative regulation of cell proliferation • gene expression • regulation of angiogenesis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
100.33 – 100.38 Mb

Chr 12:
108.86 – 108.89 Mb

PubMed search

Tryptophanyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the WARS gene.^[1]^[2]^[3]

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.^[3]

References

↑ Buwitt U, Flohr T, Bottger EC (Mar 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. PMC 556479. PMID 1537332.
↑ Fleckner J, Rasmussen HH, Justesen J (Feb 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. doi:10.1073/pnas.88.24.11520. PMC 53167. PMID 1763065.
1 2 "Entrez Gene: WARS tryptophanyl-tRNA synthetase".

Ewalt KL, Schimmel P (2002). "Activation of angiogenic signaling pathways by two human tRNA synthetases.". Biochemistry 41 (45): 13344–9. doi:10.1021/bi020537k. 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. doi:10.1002/elps.11501301199. PMID 1286667.
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. doi:10.1016/0014-5793(92)80187-L. PMID 1373391.
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.
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. doi:10.1016/0378-1119(91)90624-K. PMID 1765274.
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. doi:10.1016/0378-1119(93)90568-N. PMID 7685728.
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.
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. doi:10.1159/000134317. PMID 8646895.
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.
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.
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.
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. doi:10.1159/000056973. PMID 11474204.
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. PMC 117535. PMID 11773625.
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. PMC 117534. PMID 11773626.
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.
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.
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. PMC 139241. PMID 12477932.

PDB gallery

1o5t: Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase

1r6t: crystal structure of human tryptophanyl-tRNA synthetase

1r6u: Crystal structure of an active fragment of human tryptophanyl-tRNA synthetase with cytokine activity

1ulh: A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase

2ake: Structure of human tryptophanyl-tRNA synthetase in complex with tRNA(Trp)

2azx: Charged and uncharged tRNAs adopt distinct conformations when complexed with human tryptophanyl-tRNA synthetase

2dr2: Structure of human tryptophanyl-tRNA synthetase in complex with tRNA(Trp)

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WARS (gene)

References

Further reading