CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000771
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
60ERWNVISKSQLKNIKubiquitination[1, 2, 3, 4]
104EAKKITIKNDPSLPEubiquitination[1, 2, 4, 5]
116LPEPKCVKIGALEGYubiquitination[2]
129GYRGQRVKVFGWVHRubiquitination[2]
244IRGENMSKILKARSMacetylation[6]
244IRGENMSKILKARSMubiquitination[2, 3, 7, 8]
385NPNFQPPKRPFKRMNubiquitination[1, 4]
401SDAIVWLKEHDVKKEubiquitination[2, 7]
407LKEHDVKKEDGTFYEubiquitination[2, 7]
445CRFPVEIKSFYMQRCubiquitination[1, 2, 4]
490EEILAGYKREGIDPTubiquitination[1, 2, 3, 4, 5, 7]
507YWYTDQRKYGTCPHGubiquitination[1, 2, 4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] 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]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
  
Sequence Annotation
 MOD_RES 61 61 Phosphoserine.
 MOD_RES 244 244 N6-acetyllysine.
 MOD_RES 482 482 Phosphoserine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 548 AA 
Protein Sequence
MVLAELYVSD REGSDATGDG TKEKPFKTGL KALMTVGKEP FPTIYVDSQK ENERWNVISK 60
SQLKNIKKMW HREQMKSESR EKKEAEDSLR REKNLEEAKK ITIKNDPSLP EPKCVKIGAL 120
EGYRGQRVKV FGWVHRLRRQ GKNLMFLVLR DGTGYLQCVL ADELCQCYNG VLLSTESSVA 180
VYGMLNLTPK GKQAPGGHEL SCDFWELIGL APAGGADNLI NEESDVDVQL NNRHMMIRGE 240
NMSKILKARS MVTRCFRDHF FDRGYYEVTP PTLVQTQVEG GATLFKLDYF GEEAFLTQSS 300
QLYLETCLPA LGDVFCIAQS YRAEQSRTRR HLAEYTHVEA ECPFLTFDDL LNRLEDLVCD 360
VVDRILKSPA GSIVHELNPN FQPPKRPFKR MNYSDAIVWL KEHDVKKEDG TFYEFGEDIP 420
EAPERLMTDT INEPILLCRF PVEIKSFYMQ RCPEDSRLTE SVDVLMPNVG EIVGGSMRIF 480
DSEEILAGYK REGIDPTPYY WYTDQRKYGT CPHGGYGLGL ERFLTWILNR YHIRDVCLYP 540
RFVQRCTP 548 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0004816; F:asparagine-tRNA ligase activity; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 
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.