MARS (gene): Difference between revisions

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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{Infobox_gene}}
{{GNF_Protein_box
'''Methionyl-tRNA synthetase, cytoplasmic''' is an [[enzyme]] that in humans is encoded by the ''MARS'' [[gene]].<ref name="pmid10448063">{{cite journal |vauthors=Ubeda M, Schmitt-Ney M, Ferrer J, Habener JF | title = CHOP/GADD153 and methionyl-tRNA synthetase (MetRS) genes overlap in a conserved region that controls mRNA stability | journal = Biochem Biophys Res Commun | volume = 262 | issue = 1 | pages = 31–8 |date=Sep 1999 | pmid = 10448063 | doi = 10.1006/bbrc.1999.1140 }}</ref><ref name="entrez"/>
| image = PBB_Protein_MARS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2djv.
| PDB = {{PDB2|2djv}}
| Name = Methionyl-tRNA synthetase
| HGNCid = 6898
| Symbol = MARS
| AltSymbols =; FLJ35667; METRS; MTRNS
| OMIM = 156560
| ECnumber = 
| Homologene = 3656
| MGIid = 1345633
| GeneAtlas_image1 = PBB_GE_MARS_213671_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MARS_201475_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000049 |text = tRNA binding}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004825 |text = methionine-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:0006431 |text = methionyl-tRNA aminoacylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4141
    | Hs_Ensembl = ENSG00000166986
    | Hs_RefseqProtein = NP_004981
    | Hs_RefseqmRNA = NM_004990
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 56167344
    | Hs_GenLoc_end = 56196699
    | Hs_Uniprot = P56192
    | Mm_EntrezGene = 216443
    | Mm_Ensembl = ENSMUSG00000040354
    | Mm_RefseqmRNA = NM_001003913
    | Mm_RefseqProtein = NP_001003913
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 126699177
    | Mm_GenLoc_end = 126714627
    | Mm_Uniprot = Q68FL6
  }}
}}
'''Methionyl-tRNA synthetase''', also known as '''MARS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MARS methionyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4141| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =
| summary_text = Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene belongs to the class I family of tRNA synthetases.<ref name="entrez">{{cite web | title = Entrez Gene: MARS methionyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4141}}</ref>
| summary_text = Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene belongs to the class I family of tRNA synthetases.<ref name="entrez">{{cite web | title = Entrez Gene: MARS methionyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4141| accessdate = }}</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=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398-405 |year= 1991 |pmid= 1651330 |doi=  }}
*{{cite journal  | author=Norcum MT |title=Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15398–405 |year= 1991 |pmid= 1651330 |doi=  }}
*{{cite journal  | author=Ogata K, Kurahashi A, Kenmochi N, Terao K |title=Role of 5SrRNA as a positive effector of some aminoacyl-tRNA synthetases in macromolecular complexes, with specific reference to methionyl-tRNA synthetase. |journal=J. Biochem. |volume=110 |issue= 6 |pages= 1037-44 |year= 1992 |pmid= 1665486 |doi=  }}
*{{cite journal  |vauthors=Ogata K, Kurahashi A, Kenmochi N, Terao K |title=Role of 5SrRNA as a positive effector of some aminoacyl-tRNA synthetases in macromolecular complexes, with specific reference to methionyl-tRNA synthetase. |journal=J. Biochem. |volume=110 |issue= 6 |pages= 1037–44 |year= 1992 |pmid= 1665486 |doi=  }}
*{{cite journal  | author=Cirullo RE, Wasmuth JJ |title=Assignment of the human MARS gene, encoding methioninyl-tRNA synthetase, to chromosome 12 using human X Chinese hamster cell hybrids. |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 3 |pages= 225-34 |year= 1984 |pmid= 6585969 |doi=  }}
*{{cite journal  |vauthors=Cirullo RE, Wasmuth JJ |title=Assignment of the human MARS gene, encoding methioninyl-tRNA synthetase, to chromosome 12 using human X Chinese hamster cell hybrids. |journal=Somat. Cell Mol. Genet. |volume=10 |issue= 3 |pages= 225–34 |year= 1984 |pmid= 6585969 |doi=10.1007/BF01535245 }}
*{{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=Lage H, Dietel M |title=Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase. |journal=Gene |volume=178 |issue= 1-2 |pages= 187-9 |year= 1996 |pmid= 8921912 |doi=  }}
*{{cite journal  |vauthors=Lage H, Dietel M |title=Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase |journal=Gene |volume=178 |issue= 1–2 |pages= 187–9 |year= 1996 |pmid= 8921912 |doi=10.1016/0378-1119(96)00313-7 }}
*{{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=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=Quevillon S, Robinson JC, Berthonneau E, ''et al.'' |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183-95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316 }}
*{{cite journal   |vauthors=Quevillon S, Robinson JC, Berthonneau E, etal |title=Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein |journal=J. Mol. Biol. |volume=285 |issue= 1 |pages= 183–95 |year= 1999 |pmid= 9878398 |doi= 10.1006/jmbi.1998.2316 }}
*{{cite journal | author=Ubeda M, Schmitt-Ney M, Ferrer J, Habener JF |title=CHOP/GADD153 and methionyl-tRNA synthetase (MetRS) genes overlap in a conserved region that controls mRNA stability. |journal=Biochem. Biophys. Res. Commun. |volume=262 |issue= 1 |pages= 31-8 |year= 1999 |pmid= 10448063 |doi= 10.1006/bbrc.1999.1140 }}
*{{cite journal   |vauthors=Ko YG, Kang YS, Kim EK, etal |title=Nucleolar Localization of Human Methionyl–Trna Synthetase and Its Role in Ribosomal RNA Synthesis |journal=J. Cell Biol. |volume=149 |issue= 3 |pages= 567–74 |year= 2000 |pmid= 10791971 |doi=10.1083/jcb.149.3.567  | pmc=2174846 }}
*{{cite journal  | author=Ko YG, Kang YS, Kim EK, ''et al.'' |title=Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis. |journal=J. Cell Biol. |volume=149 |issue= 3 |pages= 567-74 |year= 2000 |pmid= 10791971 |doi=  }}
*{{cite journal   |vauthors=Kang J, Kim T, Ko YG, etal |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682–8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199 }}
*{{cite journal | author=Kang J, Kim T, Ko YG, ''et al.'' |title=Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31682-8 |year= 2000 |pmid= 10913161 |doi= 10.1074/jbc.M909965199 }}
*{{cite journal  |vauthors=Kaminska M, Shalak V, Mirande M |title=The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function |journal=Biochemistry |volume=40 |issue= 47 |pages= 14309–16 |year= 2002 |pmid= 11714285 |doi=10.1021/bi015670b }}
*{{cite journal  | author=Kaminska M, Shalak V, Mirande M |title=The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function. |journal=Biochemistry |volume=40 |issue= 47 |pages= 14309-16 |year= 2002 |pmid= 11714285 |doi=  }}
*{{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=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=Ahn HC, Kim S, Lee BJ |title=Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43 |journal=FEBS Lett. |volume=542 |issue= 1–3 |pages= 119–24 |year= 2003 |pmid= 12729910 |doi=10.1016/S0014-5793(03)00362-4 }}
*{{cite journal  | author=Ahn HC, Kim S, Lee BJ |title=Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43. |journal=FEBS Lett. |volume=542 |issue= 1-3 |pages= 119-24 |year= 2003 |pmid= 12729910 |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=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 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein–protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }}
*{{cite journal | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=4141}}
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Latest revision as of 06:09, 4 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

Methionyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the MARS gene.[1][2]

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene belongs to the class I family of tRNA synthetases.[2]

References

  1. ↑ Ubeda M, Schmitt-Ney M, Ferrer J, Habener JF (Sep 1999). "CHOP/GADD153 and methionyl-tRNA synthetase (MetRS) genes overlap in a conserved region that controls mRNA stability". Biochem Biophys Res Commun. 262 (1): 31–8. doi:10.1006/bbrc.1999.1140. PMID 10448063.
  2. ↑ 2.0 2.1 "Entrez Gene: MARS methionyl-tRNA synthetase".

Further reading



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