KARS (gene)

From Wikipedia, the free encyclopedia

Lysyl-tRNA synthetase

Identifiers

KARS; KARS2; KIAA0070

External IDs

OMIM: 601421 MGI: 1934754 HomoloGene: 4053

Gene ontology
Molecular Function:	• tRNA binding • nucleotide binding • nucleic acid binding • lysine-tRNA ligase activity • ATP binding • ligase activity
Cellular Component:	• soluble fraction • cytoplasm • mitochondrion
Biological Process:	• lysyl-tRNA aminoacylation • tRNA processing

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_005548 (mRNA)
NP_005539 (protein)

NM_053092 (mRNA)
NP_444322 (protein)

Location

Chr 16: 74.22 - 74.24 Mb

n/a

Pubmed search

[1]

[2]

Lysyl-tRNA synthetase, also known as KARS, is a human gene.^[1]

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Lysyl-tRNA synthetase is a homodimer localized to the cytoplasm which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis^[1]

[edit] References

^ ^a ^b Entrez Gene: KARS lysyl-tRNA synthetase.

[edit] Further reading

Kleiman L, Halwani R, Javanbakht H (2004). "The selective packaging and annealing of primer tRNALys3 in HIV-1.". Curr. HIV Res. 2 (2): 163-75. PMID 15078180.
Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193-205. doi:10.1089/104454904773819789. PMID 15142377.
Kleiman L, Cen S (2005). "The tRNALys packaging complex in HIV-1.". Int. J. Biochem. Cell Biol. 36 (9): 1776-86. doi:10.1016/j.biocel.2004.02.022. PMID 15183344.
Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents.". J. Biol. Chem. 266 (23): 15398-405. PMID 1651330.
Nomura N, Nagase T, Miyajima N, et al. (1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 1 (5): 223-9. PMID 7584044.
Nichols RC, Blinder J, Pai SI, et al. (1997). "Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24.". Genomics 36 (1): 210-3. doi:10.1006/geno.1996.0449. PMID 8812440.
Shiba K, Stello T, Motegi H, et al. (1997). "Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant.". J. Biol. Chem. 272 (36): 22809-16. PMID 9278442.
Stark LA, Hay RT (1998). "Human immunodeficiency virus type 1 (HIV-1) viral protein R (Vpr) interacts with Lys-tRNA synthetase: implications for priming of HIV-1 reverse transcription.". J. Virol. 72 (4): 3037-44. PMID 9525626.
Quevillon S, Robinson JC, Berthonneau E, et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein.". J. Mol. Biol. 285 (1): 183-95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
Tolkunova E, Park H, Xia J, et al. (2001). "The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript.". J. Biol. Chem. 275 (45): 35063-9. doi:10.1074/jbc.M006265200. PMID 10952987.
Cen S, Khorchid A, Javanbakht H, et al. (2001). "Incorporation of lysyl-tRNA synthetase into human immunodeficiency virus type 1.". J. Virol. 75 (11): 5043-8. doi:10.1128/JVI.75.11.5043-5048.2001. PMID 11333884.
Sang Lee J, Gyu Park S, Park H, et al. (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.
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. PMID 12477932.
Ahn HC, Kim S, Lee BJ (2003). "Solution structure and p43 binding of the p38 leucine zipper motif: coiled-coil interactions mediate the association between p38 and p43.". FEBS Lett. 542 (1-3): 119-24. PMID 12729910.
Javanbakht H, Halwani R, Cen S, et al. (2003). "The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly.". J. Biol. Chem. 278 (30): 27644-51. doi:10.1074/jbc.M301840200. PMID 12756246.
Kim MJ, Park BJ, Kang YS, et al. (2003). "Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation.". Nat. Genet. 34 (3): 330-6. doi:10.1038/ng1182. PMID 12819782.
Di Y, Li J, Zhang Y, et al. (2004). "HCC-associated protein HCAP1, a variant of GEMIN4, interacts with zinc-finger proteins.". J. Biochem. 133 (6): 713-8. PMID 12869526.