CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007810
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamate--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Glutamyl-tRNA synthetase; GluRS; P85 
Gene Name
 GUS1 
Gene Synonyms/Alias
 YGL245W; G0583; HRB724 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
36APNSIAIKLVDDKKAacetylation[1]
47DKKAPAAKLDDATEDacetylation[1]
47DKKAPAAKLDDATEDubiquitination[2]
58ATEDVFNKITSKFAAacetylation[1]
62VFNKITSKFAAIFDNacetylation[1]
72AIFDNGDKEQVAKWVacetylation[1]
77GDKEQVAKWVNLAQKacetylation[1]
89AQKELVIKNFAKLSQacetylation[1]
233QYFAQAYKGKLIIRFacetylation[1]
292VQMIKDGKAYCDDTPubiquitination[2]
350VRAKIDYKALNKTLRacetylation[1]
354IDYKALNKTLRDPVIacetylation[1]
503LIWAFNKKVIDPIAPacetylation[1]
603LNLEGDFKKTKHKLTacetylation[1]
699FFTIPDGKSVNKYGAacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By similarity). 
Sequence Annotation
 NP_BIND 437 441 ATP (By similarity).
 REGION 205 207 Glutamate binding (By similarity).
 REGION 382 386 Glutamate binding (By similarity).
 MOTIF 210 219 "HIGH" region.
 MOTIF 437 441 "KMSKS" region.
 BINDING 215 215 ATP (By similarity).
 BINDING 241 241 Glutamate (By similarity).
 BINDING 400 400 Glutamate (By similarity).
 BINDING 403 403 ATP (By similarity).
 MOD_RES 300 300 Phosphothreonine.  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 708 AA 
Protein Sequence
MPSTLTINGK APIVAYAELI AARIVNALAP NSIAIKLVDD KKAPAAKLDD ATEDVFNKIT 60
SKFAAIFDNG DKEQVAKWVN LAQKELVIKN FAKLSQSLET LDSQLNLRTF ILGGLKYSAA 120
DVACWGALRS NGMCGSIIKN KVDVNVSRWY TLLEMDPIFG EAHDFLSKSL LELKKSANVG 180
KKKETHKANF EIDLPDAKMG EVVTRFPPEP SGYLHIGHAK AALLNQYFAQ AYKGKLIIRF 240
DDTNPSKEKE EFQDSILEDL DLLGIKGDRI TYSSDYFQEM YDYCVQMIKD GKAYCDDTPT 300
EKMREERMDG VASARRDRSV EENLRIFTEE MKNGTEEGLK NCVRAKIDYK ALNKTLRDPV 360
IYRCNLTPHH RTGSTWKIYP TYDFCVPIVD AIEGVTHALR TIEYRDRNAQ YDWMLQALRL 420
RKVHIWDFAR INFVRTLLSK RKLQWMVDKD LVGNWDDPRF PTVRGVRRRG MTVEGLRNFV 480
LSQGPSRNVI NLEWNLIWAF NKKVIDPIAP RHTAIVNPVK IHLEGSEAPQ EPKIEMKPKH 540
KKNPAVGEKK VIYYKDIVVD KDDADVINVD EEVTLMDWGN VIITKKNDDG SMVAKLNLEG 600
DFKKTKHKLT WLADTKDVVP VDLVDFDHLI TKDRLEEDES FEDFLTPQTE FHTDAIADLN 660
VKDMKIGDII QFERKGYYRL DALPKDGKPY VFFTIPDGKS VNKYGAKK 708 
Gene Ontology
 GO:0017102; C:methionyl glutamyl tRNA synthetase complex; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004818; F:glutamate-tRNA ligase activity; IDA:SGD.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0006424; P:glutamyl-tRNA aminoacylation; IDA:SGD. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR004526; Glu-tRNA-synth_Ib_arc/euk.
 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.
 IPR010987; Glutathione-S-Trfase_C-like.
 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 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00987; TRNASYNTHGLU.