WARS (gene)

Tryptophanyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the WARS gene.[5][6][7]

WARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1O5T, 1R6T, 1R6U, 1ULH, 2AKE, 2AZX, 2DR2, 2QUH, 2QUI, 2QUJ, 2QUK
Identifiers
Aliases	WARS1, Tryptophanyl-tRNA synthetase, cytoplasmic, GAMMA-2, IFI53, IFP53, tryptophanyl-tRNA synthetase, HMN9, tryptophanyl-tRNA synthetase 1, WARS
External IDs	OMIM: 191050 MGI: 104630 HomoloGene: 3084 GeneCards: WARS1
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q32.2 Start 100,333,790 bp[1] End 100,376,805 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12|12 F1 Start 108,860,030 bp[2] End 108,894,174 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • aminoacyl-tRNA ligase activity • nucleotide binding • ligase activity • GO:0001948 protein binding • ATP binding • tryptophan-tRNA ligase activity • kinase inhibitor activity • protein kinase binding • protein domain specific binding • protein homodimerization activity Cellular component • extracellular exosome • cell nucleus • cytoplasm • cytosol • macromolecular complex Biological process • regulation of angiogenesis • protein biosynthesis • tRNA aminoacylation for protein translation • angiogenesis • negative regulation of cell proliferation • tryptophanyl-tRNA aminoacylation • negative regulation of protein phosphorylation • negative regulation of protein kinase activity • positive regulation of gene expression • regulation of protein ADP-ribosylation • positive regulation of protein complex assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7453	22375
Ensembl	ENSG00000140105	ENSMUSG00000021266
UniProt	P23381	P32921
RefSeq (mRNA)	NM_004184 NM_173701 NM_213645 NM_213646	NM_001164314 NM_001164488 NM_011710
RefSeq (protein)	NP_004175 NP_776049 NP_998810 NP_998811	NP_001157786 NP_001157960 NP_035840
Location (UCSC)	Chr 14: 100.33 – 100.38 Mb	Chr 12: 108.86 – 108.89 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000140105 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021266 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "Entrez Gene: WARS tryptophanyl-tRNA synthetase".

Further reading

• 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.