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{{Distinguish|Hamilton Anxiety Rating Scale}}
{{PBB_Controls
{{Infobox_gene}}
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'''Histidyl-tRNA synthetase'''  ('''HARS''') also known as [[histidine-tRNA ligase]], is an [[enzyme]] which in humans is encoded by the ''HARS'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HARS histidyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3035| accessdate = }}</ref><ref name="pmid3464104">{{cite journal | vauthors = Wasmuth JJ, Carlock LR | title = Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5 | journal = Somat. Cell Mol. Genet. | volume = 12 | issue = 5 | pages = 513–7 | year = 1986 | pmid = 3464104 | doi = 10.1007/BF01539922 }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_HARS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x59.
| PDB = {{PDB2|1x59}}
| Name = Histidyl-tRNA synthetase
| HGNCid = 4816
| Symbol = HARS
| AltSymbols =; FLJ20491; HRS
| OMIM = 142810
| ECnumber = 
| Homologene = 1592
| MGIid = 108087
| GeneAtlas_image1 = PBB_GE_HARS_202042_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004821 |text = histidine-tRNA ligase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006427 |text = histidyl-tRNA aminoacylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3035
    | Hs_Ensembl = ENSG00000170445
    | Hs_RefseqProtein = NP_002100
    | Hs_RefseqmRNA = NM_002109
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 140033675
    | Hs_GenLoc_end = 140051155
    | Hs_Uniprot = P12081
    | Mm_EntrezGene = 15115
    | Mm_Ensembl = ENSMUSG00000001380
    | Mm_RefseqmRNA = NM_008214
    | Mm_RefseqProtein = NP_032240
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 36892504
    | Mm_GenLoc_end = 36909094
    | Mm_Uniprot = Q3TKU3
  }}
}}
'''Histidyl-tRNA synthetase''', also known as '''HARS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HARS histidyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3035| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Aminoacyl-tRNA synthetases are a class of enzymes that charge [[transfer RNA|tRNA]]s with their cognate [[amino acid]]s. The protein encoded by this gene is a [[cytoplasm]]ic enzyme which belongs to the class II family of [[aminoacyl tRNA synthetases]]. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of [[histidine]] into proteins.<ref name="pmid10430027">{{cite journal | vauthors = Freist W, Verhey JF, Rühlmann A, Gauss DH, Arnez JG | title = Histidyl-tRNA synthetase | journal = Biol. Chem. | volume = 380 | issue = 6 | pages = 623–46 | year = 1999 | pmid = 10430027 | doi = 10.1515/BC.1999.079 }}</ref> The gene is located in a head-to-head orientation with [[HARS2|HARSL]] on chromosome five, where the homologous genes share a bidirectional [[promoter (biology)|promoter]].<ref name="entrez"/>
{{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 is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.<ref name="entrez">{{cite web | title = Entrez Gene: HARS histidyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3035| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
The gene product is a frequent target of [[autoantibody|autoantibodies]] in the human autoimmune disease [[polymyositis]]/[[dermatomyositis]].<ref name="pmid10430027"/>
 
== Interactions ==
 
HARS has been shown to [[Protein-protein interaction|interact]] with [[EEF1B2]]<ref name=pmid11829477>{{cite journal | vauthors = Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S | 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 }}</ref> and [[EEF1G]].<ref name=pmid11829477/>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Raben N, Borriello F, Amin J, Horwitz R, Fraser D, Plotz P | title = Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases | journal = Nucleic Acids Res. | volume = 20 | issue = 5 | pages = 1075–81 | year = 1992 | pmid = 1549469 | pmc = 312093 | doi = 10.1093/nar/20.5.1075 }}
| citations =
* {{cite journal | vauthors = Shi MH, Tsui FW, Rubin LA | title = Cellular localization of the target structures recognized by the anti-Jo-1 antibody: immunofluorescence studies on cultured human myoblasts | journal = J. Rheumatol. | volume = 18 | issue = 2 | pages = 252–8 | year = 1991 | pmid = 2023220 | doi =  }}
*{{cite journal | author=Raben N, Borriello F, Amin J, ''et al.'' |title=Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases. |journal=Nucleic Acids Res. |volume=20 |issue= 5 |pages= 1075-81 |year= 1992 |pmid= 1549469 |doi= }}
* {{cite journal | vauthors = Carlock LR, Skarecky D, Dana SL, Wasmuth JJ | title = Deletion mapping of human chromosome 5 using chromosome-specific DNA probes | journal = Am. J. Hum. Genet. | volume = 37 | issue = 5 | pages = 839–52 | year = 1985 | pmid = 2996334 | pmc = 1684692 | doi =  }}
*{{cite journal | author=Shi MH, Tsui FW, Rubin LA |title=Cellular localization of the target structures recognized by the anti-Jo-1 antibody: immunofluorescence studies on cultured human myoblasts. |journal=J. Rheumatol. |volume=18 |issue= 2 |pages= 252-8 |year= 1991 |pmid= 2023220 |doi=  }}
* {{cite journal | vauthors = Wasmuth JJ, Carlock LR | title = Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5 | journal = Somat. Cell Mol. Genet. | volume = 12 | issue = 5 | pages = 513–7 | year = 1986 | pmid = 3464104 | doi = 10.1007/BF01539922 }}
*{{cite journal | author=Carlock LR, Skarecky D, Dana SL, Wasmuth JJ |title=Deletion mapping of human chromosome 5 using chromosome-specific DNA probes. |journal=Am. J. Hum. Genet. |volume=37 |issue= 5 |pages= 839-52 |year= 1985 |pmid= 2996334 |doi=  }}
* {{cite journal | vauthors = Tsui FW, Siminovitch L | title = Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase | journal = Nucleic Acids Res. | volume = 15 | issue = 8 | pages = 3349–67 | year = 1987 | pmid = 3554142 | pmc = 340734 | doi = 10.1093/nar/15.8.3349 }}
*{{cite journal | author=Wasmuth JJ, Carlock LR |title=Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5. |journal=Somat. Cell Mol. Genet. |volume=12 |issue= 5 |pages= 513-7 |year= 1986 |pmid= 3464104 |doi= }}
* {{cite journal | vauthors = O'Hanlon TP, Raben N, Miller FW | title = A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS | journal = Biochem. Biophys. Res. Commun. | volume = 210 | issue = 2 | pages = 556–66 | year = 1995 | pmid = 7755634 | doi = 10.1006/bbrc.1995.1696 }}
*{{cite journal | author=Tsui FW, Siminovitch L |title=Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase. |journal=Nucleic Acids Res. |volume=15 |issue= 8 |pages= 3349-67 |year= 1987 |pmid= 3554142 |doi= }}
* {{cite journal | vauthors = Ogata K, Kurahashi A, Nishiyama C, Terao K | title = Presence of role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol | journal = Biochim. Biophys. Acta | volume = 1218 | issue = 3 | pages = 388–400 | year = 1994 | pmid = 8049265 | doi = 10.1016/0167-4781(94)90192-9 }}
*{{cite journal | author=O'Hanlon TP, Raben N, Miller FW |title=A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS. |journal=Biochem. Biophys. Res. Commun. |volume=210 |issue= 2 |pages= 556-66 |year= 1995 |pmid= 7755634 |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=Ogata K, Kurahashi A, Nishiyama C, Terao K |title=Presence of role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol. |journal=Biochim. Biophys. Acta |volume=1218 |issue= 3 |pages= 388-400 |year= 1994 |pmid= 8049265 |doi= }}
* {{cite journal | vauthors = Tsui HW, Mok S, de Souza L, Martin A, Tsui FW | title = Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element | journal = Gene | volume = 131 | issue = 2 | pages = 201–8 | year = 1993 | pmid = 8406012 | doi = 10.1016/0378-1119(93)90294-D }}
*{{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 = Vázquez-Abad D, Carson JH, Rothfield N | title = Localization of histidyl-tRNA synthetase (Jo-1) in human laryngeal epithelial carcinoma cell line (HEp-2 cells) | journal = Cell Tissue Res. | volume = 286 | issue = 3 | pages = 487–91 | year = 1996 | pmid = 8929351 | doi = 10.1007/s004410050718 }}
*{{cite journal | author=Tsui HW, Mok S, de Souza L, ''et al.'' |title=Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element. |journal=Gene |volume=131 |issue= 2 |pages= 201-8 |year= 1993 |pmid= 8406012 |doi= }}
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | 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=Vázquez-Abad D, Carson JH, Rothfield N |title=Localization of histidyl-tRNA synthetase (Jo-1) in human laryngeal epithelial carcinoma cell line (HEp-2 cells). |journal=Cell Tissue Res. |volume=286 |issue= 3 |pages= 487-91 |year= 1997 |pmid= 8929351 |doi= }}
* {{cite journal | vauthors = Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S | 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=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 = O'Hanlon TP, Miller FW | title = Genomic organization, transcriptional mapping, and evolutionary implications of the human bi-directional histidyl-tRNA synthetase locus (HARS/HARSL) | journal = Biochem. Biophys. Res. Commun. | volume = 294 | issue = 3 | pages = 609–14 | year = 2002 | pmid = 12056811 | doi = 10.1016/S0006-291X(02)00525-9 }}
*{{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 = Ascherman DP, Oriss TB, Oddis CV, Wright TM | title = Critical requirement for professional APCs in eliciting T cell responses to novel fragments of histidyl-tRNA synthetase (Jo-1) in Jo-1 antibody-positive polymyositis | journal = J. Immunol. | volume = 169 | issue = 12 | pages = 7127–34 | year = 2002 | pmid = 12471150 | doi = 10.4049/jimmunol.169.12.7127 }}
*{{cite journal | author=O'Hanlon TP, Miller FW |title=Genomic organization, transcriptional mapping, and evolutionary implications of the human bi-directional histidyl-tRNA synthetase locus (HARS/HARSL). |journal=Biochem. Biophys. Res. Commun. |volume=294 |issue= 3 |pages= 609-14 |year= 2002 |pmid= 12056811 |doi= 10.1016/S0006-291X(02)00525-9 }}
* {{cite journal | vauthors = Lu Q, Hope LW, Brasch M, Reinhard C, Cohen SN | title = TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 100 | issue = 13 | pages = 7626–31 | year = 2003 | pmid = 12802020 | pmc = 164637 | doi = 10.1073/pnas.0932599100 }}
*{{cite journal | author=Ascherman DP, Oriss TB, Oddis CV, Wright TM |title=Critical requirement for professional APCs in eliciting T cell responses to novel fragments of histidyl-tRNA synthetase (Jo-1) in Jo-1 antibody-positive polymyositis. |journal=J. Immunol. |volume=169 |issue= 12 |pages= 7127-34 |year= 2003 |pmid= 12471150 |doi= }}
* {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | 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=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 = Levine SM, Raben N, Xie D, Askin FB, Tuder R, Mullins M, Rosen A, Casciola-Rosen LA | title = Novel conformation of histidyl-transfer RNA synthetase in the lung: the target tissue in Jo-1 autoantibody-associated myositis | journal = Arthritis Rheum. | volume = 56 | issue = 8 | pages = 2729–39 | year = 2007 | pmid = 17665459 | doi = 10.1002/art.22790 }}
*{{cite journal | author=Lu Q, Hope LW, Brasch M, ''et al.'' |title=TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 13 |pages= 7626-31 |year= 2003 |pmid= 12802020 |doi= 10.1073/pnas.0932599100 }}
*{{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  | 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  | 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=Levine SM, Raben N, Xie D, ''et al.'' |title=Novel conformation of histidyl-transfer RNA synthetase in the lung: the target tissue in Jo-1 autoantibody-associated myositis. |journal=Arthritis Rheum. |volume=56 |issue= 8 |pages= 2729-39 |year= 2007 |pmid= 17665459 |doi= 10.1002/art.22790 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 02:09, 27 October 2017

Not to be confused with Hamilton Anxiety Rating Scale.
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

Histidyl-tRNA synthetase (HARS) also known as histidine-tRNA ligase, is an enzyme which in humans is encoded by the HARS gene.[1][2]

Function

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins.[3] The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter.[1]

Clinical significance

The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.[3]

Interactions

HARS has been shown to interact with EEF1B2[4] and EEF1G.[4]

References

  1. ↑ 1.0 1.1 "Entrez Gene: HARS histidyl-tRNA synthetase".
  2. ↑ Wasmuth JJ, Carlock LR (1986). "Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5". Somat. Cell Mol. Genet. 12 (5): 513–7. doi:10.1007/BF01539922. PMID 3464104.
  3. ↑ 3.0 3.1 Freist W, Verhey JF, Rühlmann A, Gauss DH, Arnez JG (1999). "Histidyl-tRNA synthetase". Biol. Chem. 380 (6): 623–46. doi:10.1515/BC.1999.079. PMID 10430027.
  4. ↑ 4.0 4.1 Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID 11829477.

Further reading


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