KARS - lysyl-tRNA synthetase
Entrez Gene Name: lysyl-tRNA synthetase
Entrez GeneID: Human(3735)
, Mouse(85305), Rat(292028)
, Mouse(85305), Rat(292028) Synonyms: AA589550, AL024334, AL033315, AL033367, D8Ertd698e, D8Wsu108e, KARS, KARS2, KIAA0070, KRS, LysRS, MGC94484, mKIAA0070
Gene Summary
- Human (3735): 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. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq]
Molecular Functions | Biological Process | Cellular Components | Protein Domains | Subcellular Locations | Pathways | Literature References | IPA Extras
Cell Regulation
Biological Process
diadenosine tetraphosphate biosynthetic process, lysyl-tRNA aminoacylation, translation, tRNA aminoacylation for protein translation
Literature References
- 16169070Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE. A human protein-protein interaction network: a resource for annotating the proteome.Cell 2005 Sep 23;122(6):957-68
- 17724017Kovaleski BJ, Kennedy R, Khorchid A, Kleiman L, Matsuo H, Musier-Forsyth K. Critical Role of Helix 4 of HIV-1 Capsid C-terminal Domain in Interactions with Human Lysyl-tRNA Synthetase.J Biol Chem 2007 Nov 02;282(44):32274-9
- 16702215Kovaleski BJ, Kennedy R, Hong MK, Datta SA, Kleiman L, Rein A, Musier-Forsyth K. In vitro characterization of the interaction between HIV-1 Gag and human lysyl-tRNA synthetase.J Biol Chem 2006 Jul 14;281(28):19449-56 View 127 categorized literature findings and their references in IPA
Molecular Functions
amino acid binding, aminoacyl-tRNA ligase activity, ATP binding, ligase activity, lysine-tRNA ligase activity, nucleic acid binding, nucleotide binding, protein binding, tRNA binding
Protein Domains
Aspartate-tRNA ligase, ATP binding, enzyme, Ligase, Lysine-tRNA ligase, nucleic acid binding, protein binding, tRNA ligase
