WARS (gene)

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; OMA:WARS1 - orthologs
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 108,825,956 bp [2] End 108,860,100 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte upper lobe of left lung right lung apex of heart appendix islet of Langerhans rectum epithelium of colon stromal cell of endometrium Top expressed in gastrula crypt of lieberkuhn of small intestine decidua seminal vesicula gastric mucosa mucous cell of stomach epithelium of stomach pyloric antrum medulla oblongata pontine nuclei More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aminoacyl-tRNA ligase activity nucleotide binding ligase activity 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 nucleus cytoplasm cytosol protein-containing complex Biological process regulation of angiogenesis protein biosynthesis tRNA aminoacylation for protein translation angiogenesis negative regulation of cell population 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-containing 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: 108.83 – 108.86 Mb PubMed search [3] [4]
Wikidata
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Tryptophanyl-tRNA synthetase, cytoplasmic is an aminoacyl-tRNA synthetase enzyme that attaches the amino acid tryptophan to its cognate tRNA. In humans, it is encoded by the WARS gene. ^{[5] [6] [7]}

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]

Phenylalanine Incorporation

Although WARS1 classically aminoacylates tryptophan, during states tryptophan depeletion, this enzyme has been observed to activate both tryptophan and phenylalanine. ^[8]

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, Böttger EC (February 1992). "Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor". The EMBO Journal. 11 (2): 489–496. doi:10.1002/j.1460-2075.1992.tb05079.x. PMC   556479 . PMID   1537332.
6. Fleckner J, Rasmussen HH, Justesen J (December 1991). "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". Proceedings of the National Academy of Sciences of the United States of America. 88 (24): 11520–11524. Bibcode:1991PNAS...8811520F. doi: 10.1073/pnas.88.24.11520 . PMC   53167 . PMID   1763065.
7. "Entrez Gene: WARS tryptophanyl-tRNA synthetase".
8. Pataskar A, Champagne J, Nagel R, Kenski J, Laos M, Michaux J, et al. (March 2022). "Tryptophan depletion results in tryptophan-to-phenylalanine substitutants". Nature. 603 (7902): 721–727. Bibcode:2022Natur.603..721P. doi:10.1038/s41586-022-04499-2. PMC   8942854 . PMID   35264796.

Further reading

• Ewalt KL, Schimmel P (November 2002). "Activation of angiogenic signaling pathways by two human tRNA synthetases". Biochemistry. 41 (45): 13344–13349. doi:10.1021/bi020537k. PMID   12416978.
• Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J (December 1992). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–969. doi:10.1002/elps.11501301199. PMID   1286667. S2CID   41855774.
• Bange FC, Flohr T, Buwitt U, Böttger EC (March 1992). "An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase". FEBS Letters. 300 (2): 162–166. doi:10.1016/0014-5793(92)80187-L. PMID   1373391. S2CID   35675265.
• Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP (December 1991). "Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts". The Journal of Biological Chemistry. 266 (36): 24245–24248. doi: 10.1016/S0021-9258(18)54219-8 . PMID   1761529.
• Sudomoina MA, Zinovieva OL, Kisselev LL (December 1991). "Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase". Gene. 109 (2): 291–296. doi:10.1016/0378-1119(91)90624-K. PMID   1765274.
• Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL (June 1993). "The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization". Gene. 128 (2): 237–245. doi:10.1016/0378-1119(93)90568-N. PMID   7685728.
• Popenko VI, Cherny NE, Beresten SF, Ivanova JL, Filonenko VV, Kisselev LL (December 1993). "Immunoelectron microscopic location of tryptophanyl-tRNA synthetase in mammalian, prokaryotic and archaebacterial cells". European Journal of Cell Biology. 62 (2): 248–258. PMID   7925483.
• Børglum AD, Flint T, Tommerup N, Fleckner J, Justesen J, Kruse TA (1996). "Assignment of the human tryptophanyl-tRNA synthetase gene (WARS) to chromosome 14q32.2 --> q32.32". Cytogenetics and Cell Genetics. 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]". Molekuliarnaia Biologiia. 30 (2): 319–329. PMID   8724762.
• Krause SW, Rehli M, Kreutz M, Schwarzfischer L, Paulauskis JD, Andreesen R (October 1996). "Differential screening identifies genetic markers of monocyte to macrophage maturation". Journal of Leukocyte Biology. 60 (4): 540–545. doi:10.1002/jlb.60.4.540. PMID   8864140. S2CID   24891320.
• Yuan W, Collado-Hidalgo A, Yufit T, Taylor M, Varga J (October 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". Journal of Cellular Physiology. 177 (1): 174–186. doi:10.1002/(SICI)1097-4652(199810)177:1<174::AID-JCP18>3.0.CO;2-D. PMID   9731757. S2CID   20056701.
• 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". Cytogenetics and Cell Genetics. 93 (1–2): 147–150. doi:10.1159/000056973. PMID   11474204. S2CID   2435568.
• Otani A, Slike BM, Dorrell MI, Hood J, Kinder K, Ewalt KL, et al. (January 2002). "A fragment of human TrpRS as a potent antagonist of ocular angiogenesis". Proceedings of the National Academy of Sciences of the United States of America. 99 (1): 178–183. Bibcode:2002PNAS...99..178O. doi: 10.1073/pnas.012601899 . PMC   117535 . PMID   11773625.
• Wakasugi K, Slike BM, Hood J, Otani A, Ewalt KL, Friedlander M, et al. (January 2002). "A human aminoacyl-tRNA synthetase as a regulator of angiogenesis". Proceedings of the National Academy of Sciences of the United States of America. 99 (1): 173–177. Bibcode:2002PNAS...99..173W. doi: 10.1073/pnas.012602099 . PMC   117534 . PMID   11773626.
• Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (February 2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochemical and Biophysical Research Communications. 291 (1): 158–164. doi:10.1006/bbrc.2002.6398. PMID   11829477.
• Guo Q, Gong Q, Tong KL, Vestergaard B, Costa A, Desgres J, et al. (April 2002). "Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains". The Journal of Biological Chemistry. 277 (16): 14343–14349. doi: 10.1074/jbc.M111745200 . PMID   11834741.