CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022561
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
 KIAA1352 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MAERKGTAKVDFubiquitination[1]
9AERKGTAKVDFLKKIubiquitination[1]
23IEKEIQQKWDTERVFubiquitination[1, 2]
39VNASNLEKQTSKGKYubiquitination[1, 2, 3, 4, 5]
45EKQTSKGKYFVTFPYubiquitination[1]
82GYQRLKGKCCLFPFGubiquitination[1]
98HCTGMPIKACADKLKubiquitination[1]
155AAKAGSSKYQWGIMKubiquitination[1]
162KYQWGIMKSLGLSDEubiquitination[1, 2]
193PLAIQDLKRMGLKVDubiquitination[1, 2, 4, 6]
198DLKRMGLKVDWRRSFubiquitination[1]
243RYTIYSPKDGQPCMDubiquitination[1]
268PQEYTLLKLKVLEPYubiquitination[1, 3, 5, 6]
270EYTLLKLKVLEPYPSubiquitination[1]
278VLEPYPSKLSGLKGKubiquitination[1, 3, 5, 6]
283PSKLSGLKGKNIFLVubiquitination[1]
285KLSGLKGKNIFLVAAubiquitination[1]
341MSYQGFTKDNGVVPVubiquitination[1, 2, 3, 4, 5, 6]
350NGVVPVVKELMGEEIubiquitination[1]
384MLTIKEDKGTGVVTSubiquitination[1, 2]
459QSQNDREKLAEAKEKubiquitination[1]
466KLAEAKEKIYLKGFYubiquitination[1]
483IMLVDGFKGQKVQDVubiquitination[1]
486VDGFKGQKVQDVKKTubiquitination[1]
497VKKTIQKKMIDAGDAubiquitination[1]
512LIYMEPEKQVMSRSSubiquitination[1, 2]
548KQTSQCLKNLETFCEubiquitination[1]
641VWDYVFFKEAPFPKTubiquitination[1, 2, 4]
647FKEAPFPKTQIAKEKubiquitination[1]
652FPKTQIAKEKLDQLKubiquitination[1]
659KEKLDQLKQEFEFWYubiquitination[1, 2]
716HLLLNSEKMSKSTGNubiquitination[1, 4]
719LNSEKMSKSTGNFLTubiquitination[1, 2, 4, 6]
733TLTQAIDKFSADGMRubiquitination[1, 2, 3, 4, 5, 6]
807ELNAGIIKTDQNYEKubiquitination[1, 2, 4]
814KTDQNYEKMMFKEALubiquitination[1, 2, 3, 4, 5]
818NYEKMMFKEALKTGFubiquitination[4]
822MMFKEALKTGFFEFQubiquitination[1]
832FFEFQAAKDKYRELAubiquitination[1, 2, 4]
834EFQAAKDKYRELAVEubiquitination[1]
914HDLRLRLKNYMMPAKubiquitination[1]
927AKGKKTDKQPLQKPSubiquitination[1]
965HFEANNGKLPDNKVIubiquitination[1]
983LGSMPELKKYMKKVMubiquitination[1, 2]
984GSMPELKKYMKKVMPubiquitination[1]
988ELKKYMKKVMPFVAMubiquitination[1]
1002MIKENLEKMGPRILDubiquitination[1]
1047FASEAEDKIREDCCPubiquitination[1]
1108MKMNRGIKDLSKVKLubiquitination[1]
1112RGIKDLSKVKLMRFDubiquitination[1]
1133RRVPVLGKEYTEKTPubiquitination[1]
1138LGKEYTEKTPISEHAubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs. 
Sequence Annotation
 REGION 260 509 Editing domain.
 MOTIF 53 63 "HIGH" region.
 MOTIF 716 720 "KMSKS" region.
 BINDING 719 719 ATP (By similarity).  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1176 AA 
Protein Sequence
MAERKGTAKV DFLKKIEKEI QQKWDTERVF EVNASNLEKQ TSKGKYFVTF PYPYMNGRLH 60
LGHTFSLSKC EFAVGYQRLK GKCCLFPFGL HCTGMPIKAC ADKLKREIEL YGCPPDFPDE 120
EEEEEETSVK TEDIIIKDKA KGKKSKAAAK AGSSKYQWGI MKSLGLSDEE IVKFSEAEHW 180
LDYFPPLAIQ DLKRMGLKVD WRRSFITTDV NPYYDSFVRW QFLTLRERNK IKFGKRYTIY 240
SPKDGQPCMD HDRQTGEGVG PQEYTLLKLK VLEPYPSKLS GLKGKNIFLV AATLRPETMF 300
GQTNCWVRPD MKYIGFETVN GDIFICTQKA ARNMSYQGFT KDNGVVPVVK ELMGEEILGA 360
SLSAPLTSYK VIYVLPMLTI KEDKGTGVVT SVPSDSPDDI AALRDLKKKQ ALRAKYGIRD 420
DMVLPFEPVP VIEIPGFGNL SAVTICDELK IQSQNDREKL AEAKEKIYLK GFYEGIMLVD 480
GFKGQKVQDV KKTIQKKMID AGDALIYMEP EKQVMSRSSD ECVVALCDQW YLDYGEENWK 540
KQTSQCLKNL ETFCEETRRN FEATLGWLQE HACSRTYGLG THLPWDEQWL IESLSDSTIY 600
MAFYTVAHLL QGGNLHGQAE SPLGIRPQQM TKEVWDYVFF KEAPFPKTQI AKEKLDQLKQ 660
EFEFWYPVDL RVSGKDLVPN HLSYYLYNHV AMWPEQSDKW PTAVRANGHL LLNSEKMSKS 720
TGNFLTLTQA IDKFSADGMR LALADAGDTV EDANFVEAMA DAGILRLYTW VEWVKEMVAN 780
WDSLRSGPAS TFNDRVFASE LNAGIIKTDQ NYEKMMFKEA LKTGFFEFQA AKDKYRELAV 840
EGMHRELVFR FIEVQTLLLA PFCPHLCEHI WTLLGKPDSI MNASWPVAGP VNEVLIHSSQ 900
YLMEVTHDLR LRLKNYMMPA KGKKTDKQPL QKPSHCTIYV AKNYPPWQHT TLSVLRKHFE 960
ANNGKLPDNK VIASELGSMP ELKKYMKKVM PFVAMIKENL EKMGPRILDL QLEFDEKAVL 1020
MENIVYLTNS LELEHIEVKF ASEAEDKIRE DCCPGKPLNV FRIEPGVSVS LVNPQPSNGH 1080
FSTKIEIRQG DNCDSIIRRL MKMNRGIKDL SKVKLMRFDD PLLGPRRVPV LGKEYTEKTP 1140
ISEHAVFNVD LMSKKIHLTE NGIRVDIGDT IIYLVH 1176 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004823; F:leucine-tRNA ligase activity; TAS:Reactome.
 GO:0006429; P:leucyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 
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