CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-034269
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Protein Qars 
Protein Synonyms/Alias
  
Gene Name
 Qars 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
254PYTMDLLKQHLEITGubiquitination[1]
394FEAMRKGKFAEGEATubiquitination[1]
405GEATLRMKLVMEDGKubiquitination[1]
412KLVMEDGKMDPVAYRacetylation[2]
412KLVMEDGKMDPVAYRubiquitination[1]
620FIERSDFKEESEPGYubiquitination[1]
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] 
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
 720 AA 
Protein Sequence
MATPDSLALF TGLGLSENKA RETLKNEALS TQLREAATQA HQILGSTIDK ATGVLLYDLV 60
SRLRDTRRRS FLVSYIANKK IHTGLQLSAA LEYVRSHPQD PIDTKDFEQE CGVGVVVTPE 120
QIEEAVESTI NKHQLQLLAE RYRFNMGLLM GEARAALRWA DGKMIKNEVD MQVLHLLGPK 180
MEADLVKKPK VAKARLEETD RKTAKDVVEK GEVAGQTLSL MEQLRGEALK FHKPGENYKT 240
PGYVITPYTM DLLKQHLEIT GGQVRTRFPP EPNGILHIGH AKAINFNFGY AKANNGICFL 300
RFDDTNPEKE EAKFFTAIYD MVTWLGYTPY KVTYASDYFD QLYAWAVELI HGGLAYVCHQ 360
RVEELKGHNP LPSPWRDRPK EESLLLFEAM RKGKFAEGEA TLRMKLVMED GKMDPVAYRV 420
KYTPHHRTGD KWCIYPTYDY THCLCDSIEH ITHSLCTKEF QARRSSYFWL CNALKVYCPV 480
QWEYGRLNLH YAVVSKRKIL QLVAAGAVRD WDDPRLFTLT ALRRRGFPPE AINNFCARVG 540
VTVAQTTMEP HLLEACVRDV LNDAAPRAMA VLEPLQVVIT NFPAPKPLDI RVPNFPADET 600
KGFHQVPFAS TVFIERSDFK EESEPGYKRL ASGQPVGLRH TGYVIELQNI VRGSSGCVER 660
LEVTCRRADA GEKPKAFIHW VSQPLVCEIR LYECLFQHKN PEDPVEVPGG FLSDLNPVGS 720 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 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.