CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020727
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Arginine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Arginyl-tRNA synthetase; ArgRS 
Gene Name
 Rars 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
20LQQEREIKALTAEIDubiquitination[1]
143EIAENITKHLPNNKYacetylation[2]
205FSSPNIAKEMHVGHLacetylation[2]
205FSSPNIAKEMHVGHLubiquitination[1]
278AFYKESKKRFDADEEubiquitination[1]
362VQVDDGRKIVFVPGCacetylation[3]
362VQVDDGRKIVFVPGCubiquitination[1]
393TSDLAAIKQRLFEEKubiquitination[1]
504SVAYGCIKYADLSHNacetylation[3]
629RQTGKVLKVNMWRMLacetylation[3]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1 (By similarity). 
Sequence Annotation
 REGION 1 72 Could be involved in the assembly of the
 MOTIF 201 212 "HIGH" region.
 MOD_RES 1 1 N-acetylmethionine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 660 AA 
Protein Sequence
MDGLVAQCSA RLLQQEREIK ALTAEIDRLK NCGCLEASPS LEQLREENLK LKYRLNILRR 60
SLQEERRKPT KNMININSRL QEVFGCAIRA AYPDLENPPL IVTPSQQPKF GDYQCNSAMG 120
ISQMLKAKEQ KVSPREIAEN ITKHLPNNKY IDKVEIAGPG FINVHLRKDF VSEQLTSLLV 180
NGVQLPVLGD KEKVIVDFSS PNIAKEMHVG HLRSTIIGES MSRLFEFAGY DVLRLNHVGD 240
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ AFYKESKKRF DADEEFKKRA YQCVVLLQSK 300
NPDIMKAWNL ICDVSREEFK KIYDALDITL IERGESFYQD RMKDIVKEFE DKGFVQVDDG 360
RKIVFVPGCS VPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ANKIIYVVDN GQAIHFQTIF 420
AAAQMIGWYD PKVTLVTHVG FGVVLGEDKK KFKTRSGETV RLMDLLEEGL KRSMDKLKEK 480
ERDKVLTEEE LKAAQTSVAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR 540
IRSIARLANI DEAMLQRAAR ETKIILDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 600
IYELATTFTE FYDSCYCVEK DRQTGKVLKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM 660 
Gene Ontology
 GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0034618; F:arginine binding; IEA:Compara.
 GO:0004814; F:arginine-tRNA ligase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IEA:Compara.
 GO:0006420; P:arginyl-tRNA aminoacylation; IEA:Compara. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR001278; Arg-tRNA-ligase_Ia.
 IPR015945; Arg-tRNA-synth_Ia_core.
 IPR005148; Arg-tRNA-synth_N.
 IPR008909; DALR_anticod-bd.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd. 
Pfam
 PF03485; Arg_tRNA_synt_N
 PF05746; DALR_1
 PF00750; tRNA-synt_1d 
SMART
 SM01016; Arg_tRNA_synt_N
 SM00836; DALR_1 
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR01038; TRNASYNTHARG.