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{{ distinguish|RS-24 Yars}}
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{{Infobox_gene}}
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'''Tyrosyl-tRNA synthetase, cytoplasmic''', also known as '''[[Tyrosine-tRNA ligase]]''', is an [[enzyme]] that in humans is encoded by the ''YARS'' [[gene]].<ref name="pmid8552597">{{cite journal | vauthors = Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P | title = Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria | journal = Proc Natl Acad Sci U S A | volume = 93 | issue = 1 | pages = 166–70 |date=Feb 1996 | pmid = 8552597 | pmc = 40199 | doi =10.1073/pnas.93.1.166  }}</ref><ref name="pmid9162081">{{cite journal | vauthors = Kleeman TA, Wei D, Simpson KL, First EA | title = Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine | journal = J Biol Chem | volume = 272 | issue = 22 | pages = 14420–5 |date=Jun 1997 | pmid = 9162081 | pmc = | doi =10.1074/jbc.272.22.14420  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: YARS tyrosyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8565| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
Living cells translate DNA sequences into RNA sequences and then into protein sequences. Proteins are chains of amino acids, such as tyrosine. As the protein grows, each amino acid is added to the end by an enzyme called transfer RNA (tRNA). Each amino acid has its own tRNA, and tyrosyl-tRNA synthetase is the tRNA that adds tyrosine to the end of a growing protein.  
{{GNF_Protein_box
| image = PBB_Protein_YARS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1n3l.
| PDB = {{PDB2|1n3l}}, {{PDB2|1ntg}}, {{PDB2|1q11}}
| Name = Tyrosyl-tRNA synthetase
| HGNCid = 12840
| Symbol = YARS
| AltSymbols =; CMTDIC; TYRRS; YRS; YTS
| OMIM = 603623
| ECnumber = 
| Homologene = 2730
| MGIid = 2147627
| GeneAtlas_image1 = PBB_GE_YARS_212048_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000049 |text = tRNA binding}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004831 |text = tyrosine-tRNA ligase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005153 |text = interleukin-8 receptor binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006437 |text = tyrosyl-tRNA aminoacylation}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006928 |text = cell motility}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8565
    | Hs_Ensembl = ENSG00000134684
    | Hs_RefseqProtein = NP_003671
    | Hs_RefseqmRNA = NM_003680
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 33013427
    | Hs_GenLoc_end = 33056341
    | Hs_Uniprot = P54577
    | Mm_EntrezGene = 107271
    | Mm_Ensembl = ENSMUSG00000028811
    | Mm_RefseqmRNA = XM_622904
    | Mm_RefseqProtein = XP_622904
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 128692255
    | Mm_GenLoc_end = 128721911
    | Mm_Uniprot = Q91WQ3
  }}
}}
'''Tyrosyl-tRNA synthetase''', also known as '''YARS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: YARS tyrosyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8565| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{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. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.<ref name="entrez">{{cite web | title = Entrez Gene: YARS tyrosyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8565| accessdate = }}</ref>
| summary_text = [[Aminoacyl-tRNA synthetase]]s catalyze the aminoacylation of [[transfer RNA]] (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. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. [[Cytokine]] activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an [[N-terminal]] fragment that harbors the catalytic site and a [[C-terminal]] fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.<ref name="entrez"/>
}}
}} Recently, tyrosyl-tRNA synthetase has been demonstrated as the biologically and functionally significant target for [[resveratrol]].<ref>http://www.nature.com/nature/journal/vaop/ncurrent/full/nature14028.html</ref>
 
For a comparison of [[Cytoplasm|cytoplasmic]] human tyrosyl-tRNA synthetase with its mitochondrial counterpart and with tyrosyl-tRNA synthetases of other biological kingdoms and organisms, see the Wikipedia page on [[Tyrosine-tRNA ligase]] and a general review on their structures and functions.<ref>{{cite web|last1=Bedouelle|first1=Hugues|title=Tyrosyl-tRNA Synthetases|url=https://www.ncbi.nlm.nih.gov/books/NBK6553/|website=In: Madame Curie Bioscience Database [NCBI NBK6553]|publisher=Austin (TX): Landes Bioscience}}</ref>


==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=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P |title=Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 1 |pages= 166-70 |year= 1996 |pmid= 8552597 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal  | author=Kleeman TA, Wei D, Simpson KL, First EA |title=Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. |journal=J. Biol. Chem. |volume=272 |issue= 22 |pages= 14420-5 |year= 1997 |pmid= 9162081 |doi= }}
*{{cite journal  | vauthors=Wakasugi K, Quinn CL, Tao N, Schimmel P |title=Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant |journal=EMBO J. |volume=17 |issue= 1 |pages= 297–305 |year= 1998 |pmid= 9427763 |doi= 10.1093/emboj/17.1.297 | pmc=1170380 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | vauthors=Wakasugi K, Schimmel P |title=Two distinct cytokines released from a human aminoacyl-tRNA synthetase |journal=Science |volume=284 |issue= 5411 |pages= 147–51 |year= 1999 |pmid= 10102815 |doi=10.1126/science.284.5411.147 }}
*{{cite journal  | author=Wakasugi K, Quinn CL, Tao N, Schimmel P |title=Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant. |journal=EMBO J. |volume=17 |issue= 1 |pages= 297-305 |year= 1998 |pmid= 9427763 |doi= 10.1093/emboj/17.1.297 }}
*{{cite journal  | vauthors=Wakasugi K, Schimmel P |title=Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23155–9 |year= 1999 |pmid= 10438485 |doi=10.1074/jbc.274.33.23155 }}
*{{cite journal  | author=Wakasugi K, Schimmel P |title=Two distinct cytokines released from a human aminoacyl-tRNA synthetase. |journal=Science |volume=284 |issue= 5411 |pages= 147-51 |year= 1999 |pmid= 10102815 |doi=  }}
*{{cite journal  | vauthors=Austin J, First EA |title=Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase |journal=J. Biol. Chem. |volume=277 |issue= 17 |pages= 14812–20 |year= 2002 |pmid= 11856731 |doi= 10.1074/jbc.M103396200 }}
*{{cite journal  | author=Wakasugi K, Schimmel P |title=Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase. |journal=J. Biol. Chem. |volume=274 |issue= 33 |pages= 23155-9 |year= 1999 |pmid= 10438485 |doi=  }}
*{{cite journal  | vauthors=Austin J, First EA |title=Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20243–8 |year= 2002 |pmid= 11927599 |doi= 10.1074/jbc.M201923200 }}
*{{cite journal  | author=Austin J, First EA |title=Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase. |journal=J. Biol. Chem. |volume=277 |issue= 17 |pages= 14812-20 |year= 2002 |pmid= 11856731 |doi= 10.1074/jbc.M103396200 }}
*{{cite journal   |vauthors=Wakasugi K, Slike BM, Hood J, etal |title=Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20124–6 |year= 2002 |pmid= 11956181 |doi= 10.1074/jbc.C200126200 }}
*{{cite journal  | author=Austin J, First EA |title=Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20243-8 |year= 2002 |pmid= 11927599 |doi= 10.1074/jbc.M201923200 }}
*{{cite journal  | vauthors=Austin J, First EA |title=Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28394–9 |year= 2002 |pmid= 12016229 |doi= 10.1074/jbc.M204404200 }}
*{{cite journal | author=Wakasugi K, Slike BM, Hood J, ''et al.'' |title=Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20124-6 |year= 2002 |pmid= 11956181 |doi= 10.1074/jbc.C200126200 }}
*{{cite journal  | vauthors=Yang XL, Skene RJ, McRee DE, Schimmel P |title=Crystal structure of a human aminoacyl-tRNA synthetase cytokine |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 24 |pages= 15369–74 |year= 2003 |pmid= 12427973 |doi= 10.1073/pnas.242611799 | pmc=137723 }}
*{{cite journal  | author=Austin J, First EA |title=Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 28394-9 |year= 2002 |pmid= 12016229 |doi= 10.1074/jbc.M204404200 }}
*{{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=Yang XL, Skene RJ, McRee DE, Schimmel P |title=Crystal structure of a human aminoacyl-tRNA synthetase cytokine. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 24 |pages= 15369-74 |year= 2003 |pmid= 12427973 |doi= 10.1073/pnas.242611799 }}
*{{cite journal  | vauthors=Jia J, Li B, Jin Y, Wang D |title=Expression, purification, and characterization of human tyrosyl-tRNA synthetase |journal=Protein Expr. Purif. |volume=27 |issue= 1 |pages= 104–8 |year= 2003 |pmid= 12509991 |doi=10.1016/S1046-5928(02)00576-4 }}
*{{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 }}
*{{cite journal   |vauthors=Gevaert K, Goethals M, Martens L, etal |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal  | author=Jia J, Li B, Jin Y, Wang D |title=Expression, purification, and characterization of human tyrosyl-tRNA synthetase. |journal=Protein Expr. Purif. |volume=27 |issue= 1 |pages= 104-8 |year= 2003 |pmid= 12509991 |doi=  }}
*{{cite journal   |vauthors=Jordanova A, Thomas FP, Guergueltcheva V, etal |title=Dominant intermediate Charcot-Marie-Tooth type C maps to chromosome 1p34-p35 |journal=Am. J. Hum. Genet. |volume=73 |issue= 6 |pages= 1423–30 |year= 2004 |pmid= 14606043 |doi=10.1086/379792  | pmc=1180404 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal   |vauthors=Yang XL, Otero FJ, Skene RJ, etal |title=Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 26 |pages= 15376–80 |year= 2004 |pmid= 14671330 |doi= 10.1073/pnas.2136794100 | pmc=307575 }}
*{{cite journal | author=Jordanova A, Thomas FP, Guergueltcheva V, ''et al.'' |title=Dominant intermediate Charcot-Marie-Tooth type C maps to chromosome 1p34-p35. |journal=Am. J. Hum. Genet. |volume=73 |issue= 6 |pages= 1423-30 |year= 2004 |pmid= 14606043 |doi=  }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Yang XL, Otero FJ, Skene RJ, ''et al.'' |title=Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 26 |pages= 15376-80 |year= 2004 |pmid= 14671330 |doi= 10.1073/pnas.2136794100 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=8565}}
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Latest revision as of 09:08, 16 December 2018

Not to be confused with RS-24 Yars.
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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

Tyrosyl-tRNA synthetase, cytoplasmic, also known as Tyrosine-tRNA ligase, is an enzyme that in humans is encoded by the YARS gene.[1][2][3]

Living cells translate DNA sequences into RNA sequences and then into protein sequences. Proteins are chains of amino acids, such as tyrosine. As the protein grows, each amino acid is added to the end by an enzyme called transfer RNA (tRNA). Each amino acid has its own tRNA, and tyrosyl-tRNA synthetase is the tRNA that adds tyrosine to the end of a growing protein.

Aminoacyl-tRNA synthetases catalyze the aminoacylation of transfer RNA (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. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.[3] Recently, tyrosyl-tRNA synthetase has been demonstrated as the biologically and functionally significant target for resveratrol.[4]

For a comparison of cytoplasmic human tyrosyl-tRNA synthetase with its mitochondrial counterpart and with tyrosyl-tRNA synthetases of other biological kingdoms and organisms, see the Wikipedia page on Tyrosine-tRNA ligase and a general review on their structures and functions.[5]

References

  1. ↑ Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P (Feb 1996). "Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria". Proc Natl Acad Sci U S A. 93 (1): 166–70. doi:10.1073/pnas.93.1.166. PMC 40199. PMID 8552597.
  2. ↑ Kleeman TA, Wei D, Simpson KL, First EA (Jun 1997). "Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine". J Biol Chem. 272 (22): 14420–5. doi:10.1074/jbc.272.22.14420. PMID 9162081.
  3. ↑ 3.0 3.1 "Entrez Gene: YARS tyrosyl-tRNA synthetase".
  4. ↑ http://www.nature.com/nature/journal/vaop/ncurrent/full/nature14028.html
  5. ↑ Bedouelle, Hugues. "Tyrosyl-tRNA Synthetases". In: Madame Curie Bioscience Database [NCBI NBK6553]. Austin (TX): Landes Bioscience.

Further reading



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