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Showing Protein Lysine--tRNA ligase (HMDBP00613)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 5 metabolites
Identification
HMDB Protein ID HMDBP00613
Secondary Accession Numbers
  • 5885
Name Lysine--tRNA ligase
Synonyms
  1. LysRS
  2. Lysine--tRNA ligase
  3. Lysyl-tRNA synthetase
Gene Name KARS
Protein Type Enzyme
Biological Properties
General Function Involved in nucleotide binding
Specific Function Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation.
Pathways
  • Aminoacyl-tRNA biosynthesis
Reactions
Adenosine triphosphate + L-Lysine + tRNA(Lys) → Adenosine monophosphate + Pyrophosphate + L-lysyl-tRNA(Lys) details
Adenosine triphosphate + L-Lysine + tRNA(Lys) → Adenosine monophosphate + Pyrophosphate + L-Lysyl-tRNA details
GO Classification
Biological Process
virus-host interaction
diadenosine tetraphosphate biosynthetic process
lysyl-tRNA aminoacylation
tRNA processing
Cellular Component
cytosol
mitochondrial matrix
microtubule cytoskeleton
plasma membrane
nucleus
extracellular region
aminoacyl-tRNA synthetase multienzyme complex
Component
cell part
intracellular part
cytoplasm
Function
binding
nucleotide binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
ligase activity
lysine-trna ligase activity
nucleic acid binding
ligase activity, forming carbon-oxygen bonds
ligase activity, forming aminoacyl-trna and related compounds
aminoacyl-trna ligase activity
Molecular Function
metal ion binding
ATP binding
lysine-tRNA ligase activity
amino acid binding
tRNA binding
Process
rna metabolic process
ncrna metabolic process
trna metabolic process
trna aminoacylation
trna aminoacylation for protein translation
macromolecule biosynthetic process
cellular macromolecule biosynthetic process
translation
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
lysyl-trna aminoacylation
biosynthetic process
Cellular Location
  1. Isoform Mitochondrial:Mitochondrion
Gene Properties
Chromosome Location 16
Locus 16q23.1
SNPs KARS
Gene Sequence 
>1794 bp
ATGGCGGCCGTGCAGGCGGCCGAGGTGAAAGTGGATGGCAGCGAGCCGAAACTGAGCAAG
AATGAGCTGAAGAGACGCCTGAAAGCTGAGAAGAAAGTAGCAGAGAAGGAGGCCAAACAG
AAAGAGCTCAGTGAGAAACAGCTAAGCCAAGCCACTGCTGCTGCCACCAACCACACCACT
GATAATGGTGTGGGTCCTGAGGAAGAGAGCGTGGACCCAAATCAATACTACAAAATCCGC
AGTCAAGCAATTCATCAGCTGAAGGTCAATGGGGAAGACCCATACCCACACAAGTTCCAT
GTAGACATCTCACTCACTGACTTCATCCAAAAATATAGTCACCTGCAGCCTGGGGATCAC
CTGACTGACATCACCTTAAAGGTGGCAGGTAGGATCCATGCCAAAAGAGCTTCTGGGGGA
AAGCTCATCTTCTATGATCTTCGAGGAGAGGGGGTGAAGTTGCAAGTCATGGCCAATTCC
AGAAATTATAAATCAGAAGAAGAATTTATTCATATTAATAACAAACTGCGTCGGGGAGAC
ATAATTGGAGTTCAGGGGAATCCTGGTAAAACCAAGAAGGGTGAGCTGAGCATCATTCCG
TATGAGATCACACTGCTGTCTCCCTGTTTGCATATGTTACCTCATCTTCACTTTGGCCTC
AAAGACAAGGAAACAAGGTATCGCCAGAGATACTTGGACTTGATCCTGAATGACTTTGTG
AGGCAGAAATTTATCATCCGCTCTAAGATCATCACATATATAAGAAGTTTCTTAGATGAG
CTGGGATTCCTAGAGATTGAAACTCCCATGATGAACATCATCCCAGGGGGAGCCGTGGCC
AAGCCTTTCATCACTTATCACAACGAGCTGGACATGAACTTATATATGAGAATTGCTCCA
GAACTCTATCATAAGATGCTTGTGGTTGGTGGCATCGACCGGGTTTATGAAATTGGACGC
CAGTTCCGGAATGAGGGGATTGATTTGACGCACAATCCTGAGTTCACCACCTGTGAGTTC
TACATGGCCTATGCAGACTATCACGATCTCATGGAAATCACGGAGAAGATGGTTTCAGGG
ATGGTGAAGCATATTACAGGCAGTTACAAGGTCACCTACCACCCAGATGGCCCAGAGGGC
CAAGCCTACGATGTTGACTTCACCCCACCCTTCCGGCGAATCAACATGGTAGAAGAGCTT
GAGAAAGCCCTGGGGATGAAGCTGCCAGAAACGAACCTCTTTGAAACTGAAGAAACTCGC
AAAATTCTTGATGATATCTGTGTGGCAAAAGCTGTTGAATGCCCTCCACCTCGGACCACA
GCCAGGCTCCTTGACAAGCTTGTTGGGGAGTTCCTGGAAGTGACTTGCATCAATCCTACA
TTCATCTGTGATCACCCACAGATAATGAGCCCTTTGGCTAAATGGCACCGCTCTAAAGAG
GGTCTGACTGAGCGCTTTGAGCTGTTTGTCATGAAGAAAGAGATATGCAATGCGTATACT
GAGCTGAATGATCCCATGCGGCAGCGGCAGCTTTTTGAAGAACAGGCCAAGGCCAAGGCT
GCAGGTGATGATGAGGCCATGTTCATAGATGAAAACTTCTGTACTGCCCTGGAATATGGG
CTGCCCCCCACAGCTGGCTGGGGCATGGGCATTGATCGAGTCGCCATGTTTCTCACGGAC
TCCAACAACATCAAGGAAGTACTTCTGTTTCCTGCCATGAAACCCGAAGACAAGAAGGAG
AATGTAGCAACCACTGATACACTGGAAAGCACAACAGTTGGCACTTCTGTCTAG
Protein Properties
Number of Residues 597
Molecular Weight 71496.45
Theoretical pI 6.809
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Lysyl-tRNA synthetase
MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTT
DNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH
LTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGD
IIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAP
ELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSG
MVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETR
KILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYG
LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
GenBank ID Protein 5031815
UniProtKB/Swiss-Prot ID Q15046
UniProtKB/Swiss-Prot Entry Name SYK_HUMAN
PDB IDs
GenBank Gene ID NM_005548.2
GeneCard ID KARS
GenAtlas ID KARS
HGNC ID HGNC:6215
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
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  6. Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: 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. 1994;1(5):223-9. [PubMed:7584044 ]
  7. Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [PubMed:18029264 ]
  8. Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P: Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. J Biol Chem. 1997 Sep 5;272(36):22809-16. [PubMed:9278442 ]
  9. Tolkunova E, Park H, Xia J, King MP, Davidson E: 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. 2000 Nov 10;275(45):35063-9. [PubMed:10952987 ]
  10. Zamecnik PC, Stephenson ML, Janeway CM, Randerath K: Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase. Biochem Biophys Res Commun. 1966 Jul 6;24(1):91-7. [PubMed:5338216 ]
  11. Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M: Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. J Mol Biol. 1999 Jan 8;285(1):183-95. [PubMed:9878398 ]
  12. Tan M, Wei C, Price CM: The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes. Gene. 2003 Dec 24;323:1-10. [PubMed:14659874 ]
  13. Lee YN, Nechushtan H, Figov N, Razin E: The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells. Immunity. 2004 Feb;20(2):145-51. [PubMed:14975237 ]
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  15. Halwani R, Cen S, Javanbakht H, Saadatmand J, Kim S, Shiba K, Kleiman L: Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly. J Virol. 2004 Jul;78(14):7553-64. [PubMed:15220430 ]
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