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'''Tryptophanyl-tRNA synthetase, cytoplasmic''' is an [[enzyme]] that in humans is encoded by the ''WARS'' [[gene]].<ref name="pmid1537332">{{cite journal | vauthors = Buwitt U, Flohr T, Bottger EC | title = Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor | journal = EMBO J | volume = 11 | issue = 2 | pages = 489–96 |date=Mar 1992 | pmid = 1537332 | pmc = 556479 | doi =  }}</ref><ref name="pmid1763065">{{cite journal | vauthors = Fleckner J, Rasmussen HH, Justesen J | title = 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 | journal = Proc Natl Acad Sci U S A | volume = 88 | issue = 24 | pages = 11520–4 |date=Feb 1992 | pmid = 1763065 | pmc = 53167 | doi =10.1073/pnas.88.24.11520 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: WARS tryptophanyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7453| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_WARS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1o5t.
| PDB = {{PDB2|1o5t}}, {{PDB2|1r6t}}, {{PDB2|1r6u}}, {{PDB2|1ulh}}, {{PDB2|2ake}}, {{PDB2|2azx}}, {{PDB2|2dr2}}
| Name = Tryptophanyl-tRNA synthetase
| HGNCid = 12729
| Symbol = WARS
| AltSymbols =; GAMMA-2; IFI53; IFP53
| OMIM = 191050
| ECnumber = 
| Homologene = 3084
| MGIid = 104630
| GeneAtlas_image1 = PBB_GE_WARS_200629_at_tn.png
| GeneAtlas_image2 = PBB_GE_WARS_200628_s_at_tn.png
  | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004830 |text = tryptophan-tRNA ligase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006436 |text = tryptophanyl-tRNA aminoacylation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7453
    | Hs_Ensembl = ENSG00000140105
    | Hs_RefseqProtein = NP_004175
    | Hs_RefseqmRNA = NM_004184
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 99869878
    | Hs_GenLoc_end = 99912433
    | Hs_Uniprot = P23381
    | Mm_EntrezGene = 22375
    | Mm_Ensembl =   
    | Mm_RefseqmRNA = XM_985874
    | Mm_RefseqProtein = XP_990968
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Tryptophanyl-tRNA synthetase''', also known as '''WARS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: WARS tryptophanyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7453| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: WARS tryptophanyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7453| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Ewalt KL, Schimmel P |title=Activation of angiogenic signaling pathways by two human tRNA synthetases. |journal=Biochemistry |volume=41 |issue= 45 |pages= 13344-9 |year= 2002 |pmid= 12416978 |doi=  }}
*{{cite journal  | vauthors=Ewalt KL, Schimmel P |title=Activation of angiogenic signaling pathways by two human tRNA synthetases. |journal=Biochemistry |volume=41 |issue= 45 |pages= 13344–9 |year= 2002 |pmid= 12416978 |doi=10.1021/bi020537k }}
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi=  }}
*{{cite journal   |vauthors=Rasmussen HH, van Damme J, Puype M, etal |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=10.1002/elps.11501301199 }}
*{{cite journal  | author=Bange FC, Flohr T, Buwitt U, Böttger EC |title=An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase. |journal=FEBS Lett. |volume=300 |issue= 2 |pages= 162-6 |year= 1992 |pmid= 1373391 |doi=  }}
*{{cite journal  | vauthors=Bange FC, Flohr T, Buwitt U, Böttger EC |title=An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase. |journal=FEBS Lett. |volume=300 |issue= 2 |pages= 162–6 |year= 1992 |pmid= 1373391 |doi=10.1016/0014-5793(92)80187-L }}
*{{cite journal | author=Buwitt U, Flohr T, Böttger EC |title=Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor. |journal=EMBO J. |volume=11 |issue= 2 |pages= 489-96 |year= 1992 |pmid= 1537332 |doi=  }}
*{{cite journal   |vauthors=Rubin BY, Anderson SL, Xing L, etal |title=Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. |journal=J. Biol. Chem. |volume=266 |issue= 36 |pages= 24245–8 |year= 1992 |pmid= 1761529 |doi=  }}
*{{cite journal  | author=Rubin BY, Anderson SL, Xing L, ''et al.'' |title=Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts. |journal=J. Biol. Chem. |volume=266 |issue= 36 |pages= 24245-8 |year= 1992 |pmid= 1761529 |doi=  }}
*{{cite journal  | vauthors=((Frolova LYu)), Sudomoina MA, ((Grigorieva AYu))|title=Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase. |journal=Gene |volume=109 |issue= 2 |pages= 291–6 |year= 1992 |pmid= 1765274 |doi=10.1016/0378-1119(91)90624-K |display-authors=etal}}
*{{cite journal  | author=Fleckner J, Rasmussen HH, Justesen J |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 24 |pages= 11520-4 |year= 1992 |pmid= 1763065 |doi=  }}
*{{cite journal  | vauthors=Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL |title=The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. |journal=Gene |volume=128 |issue= 2 |pages= 237–45 |year= 1993 |pmid= 7685728 |doi=10.1016/0378-1119(93)90568-N }}
*{{cite journal | author=Frolova LYu , Sudomoina MA, Grigorieva AYu, ''et al.'' |title=Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetase. |journal=Gene |volume=109 |issue= 2 |pages= 291-6 |year= 1992 |pmid= 1765274 |doi=  }}
*{{cite journal   |vauthors=Popenko VI, Cherny NE, Beresten SF, etal |title=Immunoelectron microscopic location of tryptophanyl-tRNA synthetase in mammalian, prokaryotic and archaebacterial cells. |journal=Eur. J. Cell Biol. |volume=62 |issue= 2 |pages= 248–58 |year= 1994 |pmid= 7925483 |doi=  }}
*{{cite journal | author=Frolova LY, Grigorieva AY, Sudomoina MA, Kisselev LL |title=The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. |journal=Gene |volume=128 |issue= 2 |pages= 237-45 |year= 1993 |pmid= 7685728 |doi=  }}
*{{cite journal   |vauthors=Børglum AD, Flint T, Tommerup N, etal |title=Assignment of the human tryptophanyl-tRNA synthetase gene (WARS) to chromosome 14q32.2 --> q32.32. |journal=Cytogenet. Cell Genet. |volume=73 |issue= 1-2 |pages= 99–103 |year= 1996 |pmid= 8646895 |doi=10.1159/000134317 }}
*{{cite journal  | author=Popenko VI, Cherny NE, Beresten SF, ''et al.'' |title=Immunoelectron microscopic location of tryptophanyl-tRNA synthetase in mammalian, prokaryotic and archaebacterial cells. |journal=Eur. J. Cell Biol. |volume=62 |issue= 2 |pages= 248-58 |year= 1994 |pmid= 7925483 |doi=  }}
*{{cite journal  | vauthors=Sokolova IV, Narovlianskiĭ AN, Amchenkova AM, Turpaev KT |title=[Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene] |journal=Mol. Biol. (Mosk.) |volume=30 |issue= 2 |pages= 319–29 |year= 1996 |pmid= 8724762 |doi=  }}
*{{cite journal | author=Børglum AD, Flint T, Tommerup N, ''et al.'' |title=Assignment of the human tryptophanyl-tRNA synthetase gene (WARS) to chromosome 14q32.2 --> q32.32. |journal=Cytogenet. Cell Genet. |volume=73 |issue= 1-2 |pages= 99-103 |year= 1996 |pmid= 8646895 |doi=  }}
*{{cite journal   |vauthors=Krause SW, Rehli M, Kreutz M, etal |title=Differential screening identifies genetic markers of monocyte to macrophage maturation. |journal=J. Leukoc. Biol. |volume=60 |issue= 4 |pages= 540–5 |year= 1996 |pmid= 8864140 |doi=  }}
*{{cite journal | author=Sokolova IV, Narovlianskiĭ AN, Amchenkova AM, Turpaev KT |title=[Alternative splicing of 5'-terminal exons of the human tryptophanyl-tRNA synthetase gene] |journal=Mol. Biol. (Mosk.) |volume=30 |issue= 2 |pages= 319-29 |year= 1996 |pmid= 8724762 |doi= }}
*{{cite journal   |vauthors=Yuan W, Collado-Hidalgo A, Yufit T, etal |title=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=J. Cell. Physiol. |volume=177 |issue= 1 |pages= 174–86 |year= 1998 |pmid= 9731757 |doi= 10.1002/(SICI)1097-4652(199810)177:1<174::AID-JCP18>3.0.CO;2-D }}
*{{cite journal  | author=Krause SW, Rehli M, Kreutz M, ''et al.'' |title=Differential screening identifies genetic markers of monocyte to macrophage maturation. |journal=J. Leukoc. Biol. |volume=60 |issue= 4 |pages= 540-5 |year= 1996 |pmid= 8864140 |doi=  }}
*{{cite journal  | vauthors=Jensen LL, Nielsen MM, Justesen J, Hansen LL |title=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. |journal=Cytogenet. Cell Genet. |volume=93 |issue= 1-2 |pages= 147–50 |year= 2001 |pmid= 11474204 |doi=10.1159/000056973  }}
*{{cite journal  | author=Yuan W, Collado-Hidalgo A, Yufit T, ''et al.'' |title=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=J. Cell. Physiol. |volume=177 |issue= 1 |pages= 174-86 |year= 1998 |pmid= 9731757 |doi= 10.1002/(SICI)1097-4652(199810)177:1<174::AID-JCP18>3.0.CO;2-D }}
*{{cite journal  |vauthors=Otani A, Slike BM, Dorrell MI, etal |title=A fragment of human TrpRS as a potent antagonist of ocular angiogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 178–83 |year= 2002 |pmid= 11773625 |doi= 10.1073/pnas.012601899  | pmc=117535 }}
*{{cite journal  | author=Jensen LL, Nielsen MM, Justesen J, Hansen LL |title=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. |journal=Cytogenet. Cell Genet. |volume=93 |issue= 1-2 |pages= 147-50 |year= 2001 |pmid= 11474204 |doi=  }}
*{{cite journal  |vauthors=Wakasugi K, Slike BM, Hood J, etal |title=A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 173–7 |year= 2002 |pmid= 11773626 |doi= 10.1073/pnas.012602099 | pmc=117534 }}
*{{cite journal | author=Otani A, Slike BM, Dorrell MI, ''et al.'' |title=A fragment of human TrpRS as a potent antagonist of ocular angiogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 178-83 |year= 2002 |pmid= 11773625 |doi= 10.1073/pnas.012601899 }}
*{{cite journal   |vauthors=Sang Lee J, Gyu Park S, Park H, etal |title=Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 1 |pages= 158–64 |year= 2002 |pmid= 11829477 |doi= 10.1006/bbrc.2002.6398 }}
*{{cite journal | author=Wakasugi K, Slike BM, Hood J, ''et al.'' |title=A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 1 |pages= 173-7 |year= 2002 |pmid= 11773626 |doi= 10.1073/pnas.012602099 }}
*{{cite journal   |vauthors=Guo Q, Gong Q, Tong KL, etal |title=Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14343–9 |year= 2002 |pmid= 11834741 |doi= 10.1074/jbc.M111745200 }}
*{{cite journal | author=Sang Lee J, Gyu Park S, Park H, ''et al.'' |title=Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 1 |pages= 158-64 |year= 2002 |pmid= 11829477 |doi= 10.1006/bbrc.2002.6398 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Guo Q, Gong Q, Tong KL, ''et al.'' |title=Recognition by tryptophanyl-tRNA synthetases of discriminator base on tRNATrp from three biological domains. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14343-9 |year= 2002 |pmid= 11834741 |doi= 10.1074/jbc.M111745200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7453}}
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Latest revision as of 22:27, 17 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 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.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: WARS tryptophanyl-tRNA synthetase".

Further reading



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