CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031327
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional glutamate/proline--tRNA ligase 
Protein Synonyms/Alias
 Uncharacterized protein; cDNA FLJ54314, highly similar to Glutaminyl-tRNA synthetase (EC 6.1.1.18) 
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, 2, 3, 4]
155WADGKMIKNEVDMQVubiquitination[3]
176KLEADLEKKFKVAKAubiquitination[3]
194ETDRRTAKDVVENGEubiquitination[1, 2, 3, 4]
222GEALKFHKPGENYKTubiquitination[2, 3]
228HKPGENYKTPGYVVTubiquitination[2]
243PHTMNLLKQHLEITGubiquitination[2, 3]
281NFNFGYAKANNGICFubiquitination[2, 3, 4]
355HQRGEELKGHNTLPSacetylation[5]
355HQRGEELKGHNTLPSubiquitination[1, 2, 4]
381LLFEAMRKGKFSEGEubiquitination[2, 3, 4]
383FEAMRKGKFSEGEATubiquitination[1, 2, 3, 4]
394GEATLRMKLVMEDGKubiquitination[3]
401KLVMEDGKMDPVAYRacetylation[4, 5, 6]
401KLVMEDGKMDPVAYRubiquitination[1, 2, 3, 4]
420PHHRTGDKWCIYPTYubiquitination[2, 3]
447ITHSLCTKEFQARRSubiquitination[2]
485LHYAVVSKRKILQLVubiquitination[2, 3]
575ITNFPAAKSLDIQVPacetylation[5]
575ITNFPAAKSLDIQVPubiquitination[1, 2, 4, 7, 8]
590NFPADETKGFHQVPFubiquitination[2, 3, 4]
609FIERTDFKEEPEPGFacetylation[4]
609FIERTDFKEEPEPGFubiquitination[1, 2, 3]
617EEPEPGFKRLAWGQPacetylation[4, 5]
617EEPEPGFKRLAWGQPubiquitination[1, 2, 3, 8]
641IELQHVVKGPSGCVEubiquitination[2]
748DPDSHQGKLVFNRTVubiquitination[2, 3]
758FNRTVTLKEDPGKV*acetylation[4, 5, 6]
758FNRTVTLKEDPGKV*ubiquitination[1, 2, 3, 4, 9]
763TLKEDPGKV******ubiquitination[3]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
  
Sequence Annotation
  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 764 AA 
Protein Sequence
MAALDSLSLF TSLGLSEQKA RETLKNSALS AQLREAATQA QQTLGSTIDK ATGILLYGLA 60
SRLRDTRRLS FLVSYIATAL EYVRSHPLDP IDTVDFEREC GVGVIVTPEQ IEEAVEAAIN 120
RHRPQLLVER YHFNMGLLMG EARAVLKWAD GKMIKNEVDM QVLHLLGPKL EADLEKKFKV 180
AKARLEETDR RTAKDVVENG ETADQTLSLM EQLRGEALKF HKPGENYKTP GYVVTPHTMN 240
LLKQHLEITG GQVRTRFPPE PNGILHIGHA KAINFNFGYA KANNGICFLR FDDTNPEKEE 300
AKFFTAICDM VAWLGYTPYK VTYASDYFDQ LYAWAVELIR RGLAYVCHQR GEELKGHNTL 360
PSPWRDRPME ESLLLFEAMR KGKFSEGEAT LRMKLVMEDG KMDPVAYRVK YTPHHRTGDK 420
WCIYPTYDYT HCLCDSIEHI THSLCTKEFQ ARRSSYFWLC NALDVYCPVQ WEYGRLNLHY 480
AVVSKRKILQ LVATGAVRDW DDPRLFTLTA LRRRGFPPEA INNFCARVGV TVAQTTMEPH 540
LLEACVRDVL NDTAPRAMAV LESLRVIITN FPAAKSLDIQ VPNFPADETK GFHQVPFAPI 600
VFIERTDFKE EPEPGFKRLA WGQPVGLRHT GYVIELQHVV KGPSGCVESL EVTCRRADAG 660
EKPKAFIHWV SQPLMCEVRL YERLFQHKNP EDPTEVPGGF LSDLNLASLH VVDAALVDCS 720
VALAKPFDKF QFERLGYFSV DPDSHQGKLV FNRTVTLKED PGKV 764 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004819; F:glutamine-tRNA ligase activity; IEA:InterPro.
 GO:0006425; P:glutaminyl-tRNA aminoacylation; IEA:InterPro. 
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.