CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016529
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Leucine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Leucyl-tRNA synthetase; LeuRS 
Gene Name
 Lars 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
272EYTLVKLKVLEPYPSacetylation[1]
280VLEPYPSKLSGLKGKacetylation[1, 2]
343MSYQGFTKHNGVVPVacetylation[2]
386MLTIKEDKGTGVVTSacetylation[2]
643VWDYVFFKDAPFPKTubiquitination[3]
721LNSEKMSKSTGNFLTubiquitination[3]
735TLSQAVDKFSADGMRacetylation[1]
735TLSQAVDKFSADGMRubiquitination[3]
809EMNAGIIKTDQNYEKubiquitination[3]
972NGKLPDNKVIASELGacetylation[4]
985LGSLPELKKYMKKVMacetylation[2]
985LGSLPELKKYMKKVMubiquitination[3]
1049FASEAEDKVREECCPacetylation[4]
1058REECCPGKPLNVFRTacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [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]
 [3] 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]
 [4] 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
  
Sequence Annotation
 MOTIF 55 65 "HIGH" region.
 MOTIF 718 722 "KMSKS" region.
 BINDING 721 721 ATP (By similarity).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1178 AA 
Protein Sequence
MAGRKGTAKV DFLKEIEKEA QQKWEAEKVF EVSASRLEKQ KQSSKGKYFV TFPYPYMNGR 60
LHLGHTFSLS KCEFAVGYQR LKGKSCLFPF GLHCTGMPIK ACADKLKREI ELYGCPPDFP 120
EEEEEEEESS AKPGDIVVRD KAKGKKSKAA AKAGSSKYQW DIMKSLGLSD DDIVKFSEAE 180
HWLDYFPPLA VQDLKTIGLK VDWRRSFITT DVNPYYDSFV RWQFLTLRER NKIKFGKRYT 240
IYSPKDGQPC MDHDRQTGEG VGPQEYTLVK LKVLEPYPSK LSGLKGKNIF LVAATLRPET 300
MFGQTNCWVR PDMKYIGFET ANGDIFICTQ RAARNMSYQG FTKHNGVVPV VKELMGEEIL 360
GASLSAPLTC YKVVYVLPML TIKEDKGTGV VTSVPSDSPD DLAALRDLKK KQALRTKFGI 420
RDDMVLPFEP VPVLEIPGIG NLPAVTVCDE LKIQSQNDRE KLAEAKEKLY LRGFYDGVML 480
VDGFKGQKIQ HVKKTIQKNM IDAGDALIYM EPEKQVMSRS ADECVVALCD QWYLDYGDEN 540
WKKQTFQCLK NMETFCEESR KNFEASLDWL QEHACSRTYG LGTRLPWDEQ WLIESLSDST 600
IYMAFYTVAH LLQGGDLNGQ AESPLGIRPQ QMTKDVWDYV FFKDAPFPKT QIPKEKLDQL 660
KQEFEFWYPV DLRASGKDLI PNHLSYYIYN HVAMWPEQSD KWPVSVRANG HLLLNSEKMS 720
KSTGNFLTLS QAVDKFSADG MRLALADAGD TVEDANFVEA MADAGILRLY TWVEWVKEML 780
ASCSSLRSGP ADSFNDRVFA SEMNAGIIKT DQNYEKMMFK EALKTGFFEF QAAKDKYREL 840
ATEGMHRELV FRFIEVQTIL LTPFCPHLCE HIWTLLGKPD SIMHASWPVA GPVDESLIRS 900
SQYLMEVAHD LRLRLKNYMM PAKGKKTDKQ PAQRPSHCTI YVAKNYPVWQ HITLTTLRSH 960
FEANNGKLPD NKVIASELGS LPELKKYMKK VMPFVAMIKE NMEKKGPRVL DLELEFDEQA 1020
VLMENIVYLT NSLELEHIEV KFASEAEDKV REECCPGKPL NVFRTEPGVP VSLVNPQPSS 1080
GHFSTKIDIR QGDSCESIIR RLMKTDRGIK DLSKVKLMRF DDPLLGPRRV PVLGREHSEK 1140
TLISENAVFH VDLVSKKVHL TENGLRTDIG DTMVYLVH 1178 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 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.
 IPR004493; Leu-tRNA-synth_Ia_arc/euk.
 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 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS