CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007969
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamine--tRNA ligase 
Protein Synonyms/Alias
 Glutaminyl-tRNA synthetase; GlnRS 
Gene Name
 QARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25QKARETLKNSALSAQubiquitination[1]
166WADGKMIKNEVDMQVubiquitination[1]
187KLEADLEKKFKVAKAubiquitination[1]
205ETDRRTAKDVVENGEubiquitination[1]
233GEALKFHKPGENYKTubiquitination[1]
239HKPGENYKTPGYVVTubiquitination[1]
254PHTMNLLKQHLEITGubiquitination[1]
292NFNFGYAKANNGICFubiquitination[1]
309FDDTNPEKEEAKFFTacetylation[2]
392LLFEAMRKGKFSEGEubiquitination[1]
394FEAMRKGKFSEGEATubiquitination[1, 3]
405GEATLRMKLVMEDGKubiquitination[1]
412KLVMEDGKMDPVAYRubiquitination[1]
431PHHRTGDKWCIYPTYubiquitination[1]
496LHYAVVSKRKILQLVubiquitination[1]
586ITNFPAAKSLDIQVPubiquitination[4, 5, 6]
601NFPADETKGFHQVPFubiquitination[1]
620FIERTDFKEEPEPGFacetylation[2]
620FIERTDFKEEPEPGFubiquitination[1]
628EEPEPGFKRLAWGQPubiquitination[1, 6]
759DPDSHQGKLVFNRTVubiquitination[1]
769FNRTVTLKEDPGKV*ubiquitination[1]
774TLKEDPGKV******ubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] 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]
 [6] 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
 MOTIF 270 280 "HIGH" region.
 MOTIF 493 497 "KMSKS" region.
 BINDING 496 496 ATP (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 70 70 Phosphoserine.
 MOD_RES 309 309 N6-acetyllysine.  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 775 AA 
Protein Sequence
MAALDSLSLF TSLGLSEQKA RETLKNSALS AQLREAATQA QQTLGSTIDK ATGILLYGLA 60
SRLRDTRRLS FLVSYIASKK IHTEPQLSAA LEYVRSHPLD PIDTVDFERE CGVGVIVTPE 120
QIEEAVEAAI NRHRPQLLVE RYHFNMGLLM GEARAVLKWA DGKMIKNEVD MQVLHLLGPK 180
LEADLEKKFK VAKARLEETD RRTAKDVVEN GETADQTLSL MEQLRGEALK FHKPGENYKT 240
PGYVVTPHTM NLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL 300
RFDDTNPEKE EAKFFTAICD MVAWLGYTPY KVTYASDYFD QLYAWAVELI RRGLAYVCHQ 360
RGEELKGHNT LPSPWRDRPM EESLLLFEAM RKGKFSEGEA TLRMKLVMED GKMDPVAYRV 420
KYTPHHRTGD KWCIYPTYDY THCLCDSIEH ITHSLCTKEF QARRSSYFWL CNALDVYCPV 480
QWEYGRLNLH YAVVSKRKIL QLVATGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG 540
VTVAQTTMEP HLLEACVRDV LNDTAPRAMA VLESLRVIIT NFPAAKSLDI QVPNFPADET 600
KGFHQVPFAP IVFIERTDFK EEPEPGFKRL AWGQPVGLRH TGYVIELQHV VKGPSGCVES 660
LEVTCRRADA GEKPKAFIHW VSQPLMCEVR LYERLFQHKN PEDPTEVPGG FLSDLNLASL 720
HVVDAALVDC SVALAKPFDK FQFERLGYFS VDPDSHQGKL VFNRTVTLKE DPGKV 775 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004819; F:glutamine-tRNA ligase activity; TAS:Reactome.
 GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR004514; Gln-tRNA-synth_Ib.
 IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
 IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
 IPR000924; Glu/Gln-tRNA-synth_Ib.
 IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
 IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
 IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
 IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl.
 IPR011035; Ribosomal_L25/Gln-tRNA_synth.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00749; tRNA-synt_1c
 PF03950; tRNA-synt_1c_C
 PF04558; tRNA_synt_1c_R1
 PF04557; tRNA_synt_1c_R2 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00987; TRNASYNTHGLU.