CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031036
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Asparagine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 cDNA FLJ52703, highly similar to Asparaginyl-tRNA synthetase, cytoplasmic (EC6.1.1.22) 
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
136NPNFQPPKRPFKRMNubiquitination[1]
152SDAIVWLKEHDVKKEubiquitination[2, 3, 4]
158LKEHDVKKEDGTFYEubiquitination[2, 4]
196CRFPVEIKSFYMQRCubiquitination[1, 4]
241EEILAGYKREGIDPTubiquitination[1, 2, 3, 4, 5, 6]
258YWYTDQRKYGTCPHGubiquitination[1, 4, 6]
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] 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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] 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]
 [5] 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]
 [6] 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
  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 299 AA 
Protein Sequence
MCEDWCFRDH FFDRGYYEVT PPTLVQTQVE GGATLFKLDY FGEEAFLTQS SQLYLETCLP 60
ALGDVFCIAQ SYRAEQSRTR RHLAEYTHVE AECPFLTFDD LLNRLEDLVC DVVDRILKSP 120
AGSIVHELNP NFQPPKRPFK RMNYSDAIVW LKEHDVKKED GTFYEFGEDI PEAPERLMTD 180
TINEPILLCR FPVEIKSFYM QRCPEDSRLT ESVDVLMPNV GEIVGGSMRI FDSEEILAGY 240
KREGIDPTPY YWYTDQRKYG TCPHGGYGLG LERFLTWILN RYHIRDVCLY PRFVQRCTP 299 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0004816; F:asparagine-tRNA ligase activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 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. 
Pfam
 PF00152; tRNA-synt_2 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01042; TRNASYNTHASP.