CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039899
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Arginine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
  
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
68GDLQVFYKESKKRFDubiquitination[1]
81FDTEEEFKKRAYQCVacetylation[2, 3]
94CVVLLQGKNPDITKAubiquitination[3, 4]
100GKNPDITKAWKLICDubiquitination[4]
141DRMNDIVKEFEDRGFubiquitination[1, 4]
156VQVDDGRKIVFVPGCubiquitination[4, 5]
171SIPLTIVKSDGGYTYacetylation[6]
187TSDLAAIKQRLFEEKubiquitination[1, 3, 4, 5, 7, 8]
265DLLGEGLKRSMDKLKubiquitination[1, 8]
298SVAYGCIKYADLSHNubiquitination[7]
316DYIFSFDKMLDDRGNubiquitination[1, 7]
351IDEEMLQKAARETKIubiquitination[1, 4, 7, 8]
364KILLDHEKEWKLGRCacetylation[2, 6]
364KILLDHEKEWKLGRCubiquitination[4]
367LDHEKEWKLGRCILRubiquitination[4]
449GFDILGIKPVQRM**ubiquitination[1, 3, 4, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 454 AA 
Protein Sequence
MHVGHLRSTI IGESISRLFE FAGYDVLRLN HVGDWGTQFG MLIAHLQDKF PDYLTVSPPI 60
GDLQVFYKES KKRFDTEEEF KKRAYQCVVL LQGKNPDITK AWKLICDVSR QELNKIYDAL 120
DVSLIERGES FYQDRMNDIV KEFEDRGFVQ VDDGRKIVFV PGCSIPLTIV KSDGGYTYDT 180
SDLAAIKQRL FEEKADMIIY VVDNGQSVHF QTIFAAAQMI GWYDPKVTRV FHAGFGVVLG 240
EDKKKFKTRS GETVRLMDLL GEGLKRSMDK LKEKERDKVL TAEELNAAQT SVAYGCIKYA 300
DLSHNRLNDY IFSFDKMLDD RGNTAAYLLY AFTRIRSIAR LANIDEEMLQ KAARETKILL 360
DHEKEWKLGR CILRFPEILQ KILDDLFLHT LCDYIYELAT AFTEFYDSCY CVEKDRQTGK 420
ILKVNMWRML LCEAVAAVMA KGFDILGIKP VQRM 454 
Gene Ontology
 GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:HPA.
 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; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:Compara.
 GO:0000049; F:tRNA binding; IEA:Compara.
 GO:0006420; P:arginyl-tRNA aminoacylation; IEA:Compara. 
Interpro
 IPR001278; Arg-tRNA-ligase_Ia.
 IPR015945; Arg-tRNA-synth_Ia_core.
 IPR008909; DALR_anticod-bd.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd. 
Pfam
 PF05746; DALR_1
 PF00750; tRNA-synt_1d 
SMART
 SM00836; DALR_1 
PROSITE
  
PRINTS
 PR01038; TRNASYNTHARG.