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{{Infobox_gene}}
{{PBB_Controls
'''Aspartyl-tRNA synthetase, cytoplasmic''' is an [[enzyme]] that in humans is encoded by the ''DARS'' [[gene]].<ref name="pmid2674137">{{cite journal | vauthors = Jacobo-Molina A, Peterson R, Yang DC | title = cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase | journal = J Biol Chem | volume = 264 | issue = 28 | pages = 16608–12 |date=Oct 1989 | pmid = 2674137 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DARS aspartyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1615| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of [[aminoacyl-tRNA synthetases]]. Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.<ref name="entrez"/>
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Aspartyl-tRNA synthetase
| HGNCid = 2678
| Symbol = DARS
| AltSymbols =; DKFZp781B11202; MGC111579
| OMIM = 603084
| ECnumber = 
| Homologene = 1032
| MGIid = 2442544
| GeneAtlas_image1 = PBB_GE_DARS_201624_at_tn.png
| GeneAtlas_image2 = PBB_GE_DARS_201623_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0004046 |text = aminoacylase activity}} {{GNF_GO|id=GO:0004815 |text = aspartate-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:0006422 |text = aspartyl-tRNA aminoacylation}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1615
    | Hs_Ensembl = ENSG00000115866
    | Hs_RefseqProtein = NP_001340
    | Hs_RefseqmRNA = NM_001349
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 136380724
    | Hs_GenLoc_end = 136459692
    | Hs_Uniprot = P14868
    | Mm_EntrezGene = 226414
    | Mm_Ensembl = ENSMUSG00000026356
    | Mm_RefseqmRNA = NM_145507
    | Mm_RefseqProtein = NP_663482
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 130191254
    | Mm_GenLoc_end = 130244914
    | Mm_Uniprot = Q3TF87
  }}
}}
'''Aspartyl-tRNA synthetase''', also known as '''DARS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DARS aspartyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1615| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Clinical significance ==
{{PBB_Summary
 
| section_title =
Mutations in DARS have been identified as the cause of [[leukoencephalopathy]], '''h'''ypomyelination with '''b'''rain stem and '''s'''pinal cord involvement and '''l'''eg spasticity (HBSL).<ref>{{cite journal | vauthors = Taft RJ, Vanderver A, Leventer RJ, Damiani SA, Simons C, Grimmond SM, Miller D, Schmidt J, Lockhart PJ, Pope K, Ru K, Crawford J, Rosser T, de Coo IF, Juneja M, Verma IC, Prabhakar P, Blaser S, Raiman J, Pouwels PJ, Bevova MR, Abbink TE, van der Knaap MS, Wolf NI | title=Mutations in DARS cause hypomyelination with brain stem and spinal cord involvement and leg spasticity | journal = American Journal of Human Genetics | year = 2013 | doi = 10.1016/j.ajhg.2013.04.006 | volume=92 | pages=774–780 | pmid=23643384 | pmc=3644624}}</ref>
| summary_text = Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases.  Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.<ref name="entrez">{{cite web | title = Entrez Gene: DARS aspartyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1615| accessdate = }}</ref>
 
}}
==See also==
*[[Aspartate-tRNA ligase]]


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{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=  }}
| citations =
*{{cite journal  | vauthors=Reed VS, Wastney ME, Yang DC |title=Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha. |journal=J. Biol. Chem. |volume=269 |issue= 52 |pages= 32932–6 |year= 1995 |pmid= 7806521 |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  | 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=Jacobo-Molina A, Peterson R, Yang DC |title=cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. |journal=J. Biol. Chem. |volume=264 |issue= 28 |pages= 16608-12 |year= 1989 |pmid= 2674137 |doi=  }}
*{{cite journal  | vauthors=Escalante C, Yang DC |title=Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix |journal=J. Biol. Chem. |volume=268 |issue= 8 |pages= 6014–23 |year= 1993 |pmid= 8449960 |doi=  }}
*{{cite journal  | author=Reed VS, Wastney ME, Yang DC |title=Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha. |journal=J. Biol. Chem. |volume=269 |issue= 52 |pages= 32932-6 |year= 1995 |pmid= 7806521 |doi=  }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |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 |display-authors=etal}}
*{{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=Quevillon S, Robinson JC, Berthonneau E |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 |display-authors=etal}}
*{{cite journal  | author=Escalante C, Yang DC |title=Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix. |journal=J. Biol. Chem. |volume=268 |issue= 8 |pages= 6014-23 |year= 1993 |pmid= 8449960 |doi=  }}
*{{cite journal  | vauthors=Rho SB, Kim MJ, Lee JS |title=Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 8 |pages= 4488–93 |year= 1999 |pmid= 10200289 |doi=10.1073/pnas.96.8.4488  | pmc=16359 |display-authors=etal}}
*{{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=Kang J, Kim T, Ko YG |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 |display-authors=etal}}
*{{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=Sang Lee J, Gyu Park S, Park H |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 |display-authors=etal}}
*{{cite journal  | author=Rho SB, Kim MJ, Lee JS, ''et al.'' |title=Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 8 |pages= 4488-93 |year= 1999 |pmid= 10200289 |doi=  }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
*{{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=Cheong HK, Park JY, Kim EH |title=Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function |journal=Int. J. Biochem. Cell Biol. |volume=35 |issue= 11 |pages= 1548–57 |year= 2004 |pmid= 12824064 |doi=10.1016/S1357-2725(03)00070-0 |display-authors=etal}}
*{{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=Bouwmeester T, Bauch A, Ruffner H |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97–105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 |display-authors=etal}}
*{{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=Gerhard DS, Wagner L, Feingold EA |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 |display-authors=etal}}
*{{cite journal  | author=Cheong HK, Park JY, Kim EH, ''et al.'' |title=Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function. |journal=Int. J. Biochem. Cell Biol. |volume=35 |issue= 11 |pages= 1548-57 |year= 2004 |pmid= 12824064 |doi=  }}
*{{cite journal  | vauthors=Bonnefond L, Fender A, Rudinger-Thirion J |title=Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS |journal=Biochemistry |volume=44 |issue= 12 |pages= 4805–16 |year= 2005 |pmid= 15779907 |doi= 10.1021/bi047527z |display-authors=etal}}
*{{cite journal  | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal  | vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |display-authors=etal}}
*{{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=Tu LC, Yan X, Hood L, Lin B |title=Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells |journal=Mol. Cell. Proteomics |volume=6 |issue= 4 |pages= 575–88 |year= 2007 |pmid= 17220478 |doi= 10.1074/mcp.M600249-MCP200 }}
*{{cite journal  | author=Bonnefond L, Fender A, Rudinger-Thirion J, ''et al.'' |title=Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. |journal=Biochemistry |volume=44 |issue= 12 |pages= 4805-16 |year= 2005 |pmid= 15779907 |doi= 10.1021/bi047527z }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Tu LC, Yan X, Hood L, Lin B |title=Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells. |journal=Mol. Cell Proteomics |volume=6 |issue= 4 |pages= 575-88 |year= 2007 |pmid= 17220478 |doi= 10.1074/mcp.M600249-MCP200 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 18:14, 30 August 2017

VALUE_ERROR (nil)
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

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

Aspartyl-tRNA synthetase (DARS) is part of a multienzyme complex of aminoacyl-tRNA synthetases. Aspartyl-tRNA synthetase charges its cognate tRNA with aspartate during protein biosynthesis.[2]

Clinical significance

Mutations in DARS have been identified as the cause of leukoencephalopathy, hypomyelination with brain stem and spinal cord involvement and leg spasticity (HBSL).[3]

See also

References

  1. ↑ Jacobo-Molina A, Peterson R, Yang DC (Oct 1989). "cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase". J Biol Chem. 264 (28): 16608–12. PMID 2674137.
  2. ↑ 2.0 2.1 "Entrez Gene: DARS aspartyl-tRNA synthetase".
  3. ↑ Taft RJ, Vanderver A, Leventer RJ, Damiani SA, Simons C, Grimmond SM, Miller D, Schmidt J, Lockhart PJ, Pope K, Ru K, Crawford J, Rosser T, de Coo IF, Juneja M, Verma IC, Prabhakar P, Blaser S, Raiman J, Pouwels PJ, Bevova MR, Abbink TE, van der Knaap MS, Wolf NI (2013). "Mutations in DARS cause hypomyelination with brain stem and spinal cord involvement and leg spasticity". American Journal of Human Genetics. 92: 774–780. doi:10.1016/j.ajhg.2013.04.006. PMC 3644624. PMID 23643384.

Further reading


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