HARS2
From Wikipedia, the free encyclopedia
| Histidyl-tRNA synthetase 2, mitochondrial (putative) | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | HARS2; HARSL; HARSR; HO3 | ||||||||||||
| External IDs | OMIM: 600783 MGI: 1918041 HomoloGene: 40819 GeneCards: HARS2 Gene | ||||||||||||
| EC number | 6.1.1.21 | ||||||||||||
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| RNA expression pattern | |||||||||||||
| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 23438 | 70791 | |||||||||||
| Ensembl | ENSG00000112855 | ENSMUSG00000019143 | |||||||||||
| UniProt | P49590 | Q99KH0 | |||||||||||
| RefSeq (mRNA) | NM_012208 | NM_080636.1 | |||||||||||
| RefSeq (protein) | NP_036340 | NP_542367.1 | |||||||||||
| Location (UCSC) | Chr 5: 140.07 – 140.08 Mb |
Chr 18: 36.94 – 36.95 Mb |
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| PubMed search | [1] | [2] | |||||||||||
Probable histidyl-tRNA synthetase, mitochondrial is an enzyme that in humans is encoded by the HARS2 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 is an enzyme belonging to the class II family of aminoacyl-tRNA synthetases. Functioning in the synthesis of histidyl-transfer RNA, the enzyme plays an accessory role in the regulation of protein biosynthesis. The gene is located in a head-to-head orientation with HARS on chromosome five, where the homologous genes share a bidirectional promoter.[2]
[edit] References
- ^ O'Hanlon TP, Raben N, Miller FW (Jun 1995). "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". Biochem Biophys Res Commun 210 (2): 556–66. doi:10.1006/bbrc.1995.1696. PMID 7755634.
- ^ a b "Entrez Gene: HARS2 histidyl-tRNA synthetase 2, mitochondrial (putative)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23438.
[edit] Further reading
- Freist W, Verhey JF, Rühlmann A, et al. (1999). "Histidyl-tRNA synthetase.". Biol. Chem. 380 (6): 623–46. doi:10.1515/BC.1999.079. PMID 10430027.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Lama J, Trono D (1998). "Human immunodeficiency virus type 1 matrix protein interacts with cellular protein HO3.". J. Virol. 72 (2): 1671–6. PMC 124654. PMID 9445076. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=124654.
- Tsui HW, Mok S, de Souza L, et al. (1993). "Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element.". Gene 131 (2): 201–8. doi:10.1016/0378-1119(93)90294-D. PMID 8406012.
- Raben N, Borriello F, Amin J, et al. (1992). "Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases.". Nucleic Acids Res. 20 (5): 1075–81. doi:10.1093/nar/20.5.1075. PMC 312093. PMID 1549469. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=312093.
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