CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020647
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable glutamate--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Glutamyl-tRNA synthetase; GluRS 
Gene Name
 Ears2 
Gene Synonyms/Alias
 Kiaa1970 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
151PQRLELLKKEALRSRacetylation[1]
256EWLVSTSKHLLLYQAacetylation[2]
256EWLVSTSKHLLLYQAsuccinylation[2]
284LLNRDGSKLSKRQGDacetylation[1]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
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 284 288 ATP (By similarity).
 REGION 40 42 Glutamate binding (By similarity).
 REGION 228 232 Glutamate binding (By similarity).
 MOTIF 45 53 "HIGH" region.
 MOTIF 284 288 "KMSKS" region.
 BINDING 50 50 ATP (By similarity).
 BINDING 76 76 Glutamate (By similarity).
 BINDING 246 246 Glutamate (By similarity).
 BINDING 249 249 ATP (By similarity).
 MOD_RES 486 486 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 523 AA 
Protein Sequence
MAAPLKRLLL AEPHVVALGH RVGRREASLG PDPGAPVRVR FAPSPTGFLH LGGLRTALYN 60
YIFAKKHQGS FILRLEDTDQ SRLVPGAAES IEDMLEWAGI PPDESPRRGG PAGPYCQSQR 120
LALYAQATEA LLRSGAAYPC FCLPQRLELL KKEALRSRQT PRYDNRCRNL SQAQVAQKLA 180
VDPKPAIRFR LEEAVPAFQD LVYGWTQHEV ASVEGDPVIL KSDGFPTYHL ACVVDDHHMS 240
ISHVLRGSEW LVSTSKHLLL YQALGWQPPR FAHLPLLLNR DGSKLSKRQG DIFLEHFAAT 300
GFLPEALLDI ITNCGSGFAE NQMGRTLPEL ITQFDLTRIT CHSALLDLEK LPEFNRLHLR 360
RLVSSETQRP QLVEKLQGLV KEAFGSELQN KDVLDPAYME RILLLRQGHI SRLQDLVSPV 420
YSYLWTRPAV HRSELGASSE NVDVIAKRLL GLLERPGLSL TQDVLNRELK KLSEGLEGAK 480
HSSVMKLLRM ALSGQLQGPP VAEMMVSLGP KEVRERIQKV LSS 523 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004818; F:glutamate-tRNA ligase activity; IEA:EC.
 GO:0050561; F:glutamate-tRNA(Gln) ligase activity; IEA:Compara.
 GO:0000049; F:tRNA binding; IEA:InterPro.
 GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:Compara.
 GO:0070127; P:tRNA aminoacylation for mitochondrial protein translation; IEA:Compara. 
Interpro
 IPR008925; aa-tRNA-synth_I_codon-bd.
 IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
 IPR001412; aa-tRNA-synth_I_CS.
 IPR004527; Glu-tRNA-ligase_Ib_bac/mito.
 IPR000924; Glu/Gln-tRNA-synth_Ib.
 IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
 IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00749; tRNA-synt_1c 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00987; TRNASYNTHGLU.