WARS (gene)

From Wikipedia, the free encyclopedia

Tryptophanyl-tRNA synthetase

PDB rendering based on 1o5t.

Available structures: 1o5t, 1r6t, 1r6u, 1ulh, 2ake, 2azx, 2dr2

Identifiers

Symbol(s)

WARS; GAMMA-2; IFI53; IFP53

External IDs

OMIM: 191050 MGI: 104630 HomoloGene: 3084

Gene ontology
Molecular Function:	• nucleotide binding • tryptophan-tRNA ligase activity • ATP binding • ligase activity
Cellular Component:	• soluble fraction • cytoplasm
Biological Process:	• tryptophanyl-tRNA aminoacylation • negative regulation of cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_004184 (mRNA)
NP_004175 (protein)

XM_985874 (mRNA)
XP_990968 (protein)

Location

Chr 14: 99.87 - 99.91 Mb

n/a

Pubmed search

[1]

[2]

Tryptophanyl-tRNA synthetase, also known as WARS, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: WARS tryptophanyl-tRNA synthetase.

[edit] 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.
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.
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.
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.
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.
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.
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.
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. 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. 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. 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. 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. PMID 12477932.