CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008837
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20LQQEEEIKSLTAEIDubiquitination[1, 2, 3, 4, 5]
30TAEIDRLKNCGCLGAubiquitination[4]
60YRLNILRKSLQAERNacetylation[6]
193PALGENKKVIVDFSSubiquitination[4, 7]
205FSSPNIAKEMHVGHLacetylation[6, 7, 8, 9]
205FSSPNIAKEMHVGHLubiquitination[1, 4, 5, 7, 10]
274GDLQVFYKESKKRFDubiquitination[2]
287FDTEEEFKKRAYQCVacetylation[6]
300CVVLLQGKNPDITKAubiquitination[4]
306GKNPDITKAWKLICDubiquitination[4]
347DRMNDIVKEFEDRGFubiquitination[2, 4]
362VQVDDGRKIVFVPGCubiquitination[1, 4, 5, 10]
393TSDLAAIKQRLFEEKubiquitination[1, 2, 4, 5, 10]
471DLLGEGLKRSMDKLKubiquitination[2]
522DYIFSFDKMLDDRGNubiquitination[2]
557IDEEMLQKAARETKIubiquitination[2, 4]
570KILLDHEKEWKLGRCubiquitination[4]
573LDHEKEWKLGRCILRubiquitination[4]
655GFDILGIKPVQRM**ubiquitination[2, 4, 10]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] 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]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
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. 
Sequence Annotation
 REGION 1 72 Could be involved in the assembly of the
 MOTIF 201 212 "HIGH" region.
 MOD_RES 1 1 N-acetylmethionine.  
Keyword
 Acetylation; Alternative initiation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 660 AA 
Protein Sequence
MDVLVSECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASPN LEQLQEENLK LKYRLNILRK 60
SLQAERNKPT KNMINIISRL QEVFGHAIKA AYPDLENPPL LVTPSQQAKF GDYQCNSAMG 120
ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC IEKVEIAGPG FINVHLRKDF VSEQLTSLLV 180
NGVQLPALGE NKKVIVDFSS PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHVGD 240
WGTQFGMLIA HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK 300
NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD RMNDIVKEFE DRGFVQVDDG 360
RKIVFVPGCS IPLTIVKSDG GYTYDTSDLA AIKQRLFEEK ADMIIYVVDN GQSVHFQTIF 420
AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK KFKTRSGETV RLMDLLGEGL KRSMDKLKEK 480
ERDKVLTAEE LNAAQTSVAY GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR 540
IRSIARLANI DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 600
IYELATAFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD ILGIKPVQRM 660 
Gene Ontology
 GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0034618; F:arginine binding; IEA:Compara.
 GO:0004814; F:arginine-tRNA ligase activity; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IEA:Compara.
 GO:0006420; P:arginyl-tRNA aminoacylation; TAS:ProtInc. 
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.