CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018162
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Probable leucine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Leucyl-tRNA synthetase; LeuRS 
Gene Name
 Lars2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
67KWWHQQIKEQASRVSacetylation[1]
78SRVSEEDKLKPKFYLacetylation[2]
154SWTQSNIKHMRKQLDacetylation[3]
Reference
 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] 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]
 [3] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
  
Sequence Annotation
 MOTIF 91 101 "HIGH" region.
 MOTIF 638 642 "KMSKS" region.
 BINDING 641 641 ATP (By similarity).
 MOD_RES 235 235 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 902 AA 
Protein Sequence
MASTCQRLSF YVSPLKRQLV SRPPVILWER LIPGCSRSIY SATGKWTKEY TLQTRKDVEK 60
WWHQQIKEQA SRVSEEDKLK PKFYLLSMFP YPSGKLHMGH VRVYTLSDTI ARFQKMRGMQ 120
VINPMGWDAF GLPAENAAIE RNLHPESWTQ SNIKHMRKQL DRLGLCFSWD REITTCLPDY 180
YKWTQYLFIK LYEAGLAYQK EALVNWDPVD QTVLANEQVN EYGCSWRSGA KVEKKYLRQW 240
FIKTTAYAKA MQDALADLPE WYGIKGMQAH WIGDCVGCHL DFTLKVDGED TGEKLTAYTA 300
TPEAIYGISH VAISPSHGLL HGCSSVKKAL QKALVPGRDC LTPVMAVSML TLQEVPIVIM 360
ANPDLEGSLD SKIGIPSTSS EDTRLAQALG LPYSEVIEAS PDGTERLSGS AEFTGMTRQD 420
AFVALTRKAR GMRVGGHVTS NKLKDWLISR QRYWGTPIPI VHCPACGPVP VPLQDLPVIL 480
PSIASLTGRG GSPLATALEW VNCSCPRCKG SAKRETDTMD TFVDSAWYYF RYTDPHNTQS 540
PFGSALADFW MPVDLYIGGK EHAVMHLFYA RFLSHFCHDQ KMVKHREPFH KLLAQGLIKG 600
QTFRLPSGQC LKKEDIDFTG PAPVCAKTKE KLEVTWEKMS KSKHNGVDPE EIVAQYGIDT 660
IRLYILFAAP PEKDILWDVK TDALPGVLRW QQRLWSLTTR FIEARTSGTV PQPQLLNSKE 720
KTKAQNLWEY KNAVIAQVTT HFTEDFALNS VVSQLMGLSS ALSQASQRVV LHSPEFEDAL 780
CALLVMAAPL APHVTSELWA GLTLVPSKLC DHYAWDSGVM LQAWPTVDSQ FLQKPDMVQM 840
AVLINNKACG KIPVPQHVAQ DQDKVHELVL QSELGMKLLQ GRSIKKAFLS PRTALINFLV 900
QE 902 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004823; F:leucine-tRNA ligase activity; IEA:EC.
 GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR002302; Leu-tRNA-ligase_bac/mito.
 IPR025709; Leu_tRNA-synth_edit.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd.
 IPR013155; V/L/I-tRNA-synth_anticodon-bd.
 IPR009008; Val/Leu/Ile-tRNA-synth_edit. 
Pfam
 PF08264; Anticodon_1
 PF00133; tRNA-synt_1
 PF13603; tRNA-synt_1_2 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00985; TRNASYNTHLEU.