CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016546
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Asparagine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Asparaginyl-tRNA synthetase; AsnRS 
Gene Name
 Nars 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
49KALMTVGKEPFPTIYubiquitination[1]
71ERWDVISKSQMKNIKacetylation[2]
71ERWDVISKSQMKNIKsuccinylation[2]
115EAKKIIIKNDPSLPEacetylation[3]
115EAKKIIIKNDPSLPEubiquitination[1]
140GYRGQRVKVFGWVHRacetylation[3]
255IRGENMSKILKARSMacetylation[3]
255IRGENMSKILKARSMubiquitination[1]
393YELNPNFKPPKRPFRubiquitination[1]
456CRFPVEIKSFYMQRCubiquitination[1]
501EEILEGYKREGIDPAacetylation[2]
501EEILEGYKREGIDPAubiquitination[1]
518YWYTDQRKYGTCPHGacetylation[3]
Reference
 [1] 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]
 [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]
 [3] 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
Functional Description
  
Sequence Annotation
 MOD_RES 72 72 Phosphoserine (By similarity).
 MOD_RES 255 255 N6-acetyllysine (By similarity).
 MOD_RES 493 493 Phosphoserine.  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 559 AA 
Protein Sequence
MSSEVIRGTA EMVLAELYVS DREGNDATGD GTKEKPFKTG LKALMTVGKE PFPTIYVDSQ 60
KENERWDVIS KSQMKNIKKM WHREQMKNDS REKKEAEDNL RREKNLEEAK KIIIKNDPSL 120
PEPACVKISA LEGYRGQRVK VFGWVHRLRR QGKNLMFLVL RDGTGYLQCV LSDDLCQCYN 180
GVVLSTESSV AVYGTLNLTP KGKQAPGGHE LSCDFWELVG LAPAGGADNL INEESDVDVQ 240
LNNRHMMIRG ENMSKILKAR SMITRCFRDH FFDRGYCEVT TPTLVQTQVE GGATLFKLDY 300
FGEEAFLTQS SQLYLETCLP ALGDVFCIAQ SYRAEQSRTR RHLAEFTHVE AECPFLTFED 360
LLNRLEDLVC DVVDRVLKSP VASIVYELNP NFKPPKRPFR RMNYSDAIEW LKEHDVKKED 420
GTFYEFGDDI PEAPERLMTD TINEPILLCR FPVEIKSFYM QRCPEDPRLT ESVDVLMPNV 480
GEIVGGSMRS WDSEEILEGY KREGIDPAPY YWYTDQRKYG TCPHGGYGLG LERFLSWILN 540
RYHIRDVCLY PRFLQRCRP 559 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004816; F:asparagine-tRNA ligase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR004364; aa-tRNA-synt_II.
 IPR018150; aa-tRNA-synt_II-like.
 IPR006195; aa-tRNA-synth_II.
 IPR004522; Asn-tRNA-ligase_IIb.
 IPR002312; Asp/Asn-tRNA-synth_IIb.
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase. 
Pfam
 PF00152; tRNA-synt_2
 PF01336; tRNA_anti 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01042; TRNASYNTHASP.