- KARS (gene)
Lysyl-tRNA synthetase, also known as KARS, is a human
gene .cite web | title = Entrez Gene: KARS lysyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3735| accessdate = ]PBB_Summary
section_title =
summary_text = 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 dermatomyositiscite web | title = Entrez Gene: KARS lysyl-tRNA synthetase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3735| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Kleiman L, Halwani R, Javanbakht H |title=The selective packaging and annealing of primer tRNALys3 in HIV-1. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 163–75 |year= 2004 |pmid= 15078180 |doi=
*cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193–205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789
*cite journal | author=Kleiman L, Cen S |title=The tRNALys packaging complex in HIV-1. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 9 |pages= 1776–86 |year= 2005 |pmid= 15183344 |doi= 10.1016/j.biocel.2004.02.022
*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=Nomura N, Nagase T, Miyajima N, "et al." |title=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. |journal=DNA Res. |volume=1 |issue= 5 |pages= 223–9 |year= 1995 |pmid= 7584044 |doi=
*cite journal | author=Nichols RC, Blinder J, Pai SI, "et al." |title=Assignment of two human autoantigen genes-isoleucyl-tRNA synthetase locates to 9q21 and lysyl-tRNA synthetase locates to 16q23-q24. |journal=Genomics |volume=36 |issue= 1 |pages= 210–3 |year= 1997 |pmid= 8812440 |doi= 10.1006/geno.1996.0449
*cite journal | author=Shiba K, Stello T, Motegi H, "et al." |title=Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. |journal=J. Biol. Chem. |volume=272 |issue= 36 |pages= 22809–16 |year= 1997 |pmid= 9278442 |doi=
*cite journal | author=Stark LA, Hay RT |title=Human immunodeficiency virus type 1 (HIV-1) viral protein R (Vpr) interacts with Lys-tRNA synthetase: implications for priming of HIV-1 reverse transcription. |journal=J. Virol. |volume=72 |issue= 4 |pages= 3037–44 |year= 1998 |pmid= 9525626 |doi=
*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 | author=Tolkunova E, Park H, Xia J, "et al." |title=The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript. |journal=J. Biol. Chem. |volume=275 |issue= 45 |pages= 35063–9 |year= 2001 |pmid= 10952987 |doi= 10.1074/jbc.M006265200
*cite journal | author=Cen S, Khorchid A, Javanbakht H, "et al." |title=Incorporation of lysyl-tRNA synthetase into human immunodeficiency virus type 1. |journal=J. Virol. |volume=75 |issue= 11 |pages= 5043–8 |year= 2001 |pmid= 11333884 |doi= 10.1128/JVI.75.11.5043-5048.2001
*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 | 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 | 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 | author=Javanbakht H, Halwani R, Cen S, "et al." |title=The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly. |journal=J. Biol. Chem. |volume=278 |issue= 30 |pages= 27644–51 |year= 2003 |pmid= 12756246 |doi= 10.1074/jbc.M301840200
*cite journal | author=Kim MJ, Park BJ, Kang YS, "et al." |title=Downregulation of FUSE-binding protein and c-myc by tRNA synthetase cofactor p38 is required for lung cell differentiation. |journal=Nat. Genet. |volume=34 |issue= 3 |pages= 330–6 |year= 2003 |pmid= 12819782 |doi= 10.1038/ng1182
*cite journal | author=Di Y, Li J, Zhang Y, "et al." |title=HCC-associated protein HCAP1, a variant of GEMIN4, interacts with zinc-finger proteins. |journal=J. Biochem. |volume=133 |issue= 6 |pages= 713–8 |year= 2004 |pmid= 12869526 |doi=PBB_Controls
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