CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018665
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Aspartyl-tRNA synthetase; AspRS 
Gene Name
 Dars 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
74HTSRAKGKQCFLVLRubiquitination[1]
99AVGDHASKQMVKFAAubiquitination[1]
103HASKQMVKFAANINKacetylation[2]
103HASKQMVKFAANINKubiquitination[1]
110KFAANINKESIIDVEubiquitination[1]
241VFTVSYFKNNAYLAQubiquitination[1]
330TEIQTVSKQFPCEPFubiquitination[1]
383LGRLVKEKYDTDFYVubiquitination[1]
411MPDPRNPKQSNSYDMubiquitination[1]
451HHGIDLEKIKAYIDSacetylation[3]
451HHGIDLEKIKAYIDSubiquitination[1]
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] 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] 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
 Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 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. 
Sequence Annotation
 MOD_RES 74 74 N6-acetyllysine (By similarity).
 MOD_RES 249 249 Phosphoserine (By similarity).
 MOD_RES 374 374 N6-acetyllysine (By similarity).  
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
 501 AA 
Protein Sequence
MPSTNASRKG QEKPREIVDA AEDYAKERYG ISSMIQSQEK PDRVLVRVKD LTVQKADDVV 60
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIIDVEGVV 120
RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAI RPEVEGEEDG RATVNQDTRL 180
DNRVIDLRTS TSQAIFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF 240
KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 300
EVVEEIADTL VQIFKGLQER FQTEIQTVSK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV 360
EMDDEEDLST PNEKLLGRLV KEKYDTDFYV LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 420
RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF 480
LGLHNVRQTS MFPRDPKRLT P 501 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004815; F:aspartate-tRNA ligase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR004364; aa-tRNA-synt_II.
 IPR018150; aa-tRNA-synt_II-like.
 IPR006195; aa-tRNA-synth_II.
 IPR004523; Asp-tRNA_synthase.
 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.