CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004267
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Aspartyl-tRNA synthetase; AspRS; Cell proliferation-inducing gene 40 protein 
Gene Name
 DARS 
Gene Synonyms/Alias
 PIG40 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26DAAEDYAKERYGISSubiquitination[1]
40SMIQSQEKPDRVLVRubiquitination[1]
74HTSRAKGKQCFLVLRacetylation[2]
74HTSRAKGKQCFLVLRubiquitination[1]
99AVGDHASKQMVKFAAubiquitination[3, 4, 5, 6]
103HASKQMVKFAANINKubiquitination[3, 6, 7]
110KFAANINKESIVDVEubiquitination[1]
241VFTVSYFKNNAYLAQubiquitination[5]
330TEIQTVNKQFPCEPFubiquitination[1, 3, 6]
338QFPCEPFKFLEPTLRubiquitination[1]
374DLSTPNEKLLGHLVKacetylation[2]
374DLSTPNEKLLGHLVKubiquitination[1, 4]
411MPDPRNPKQSNSYDMubiquitination[1, 8]
451HHGIDLEKIKAYIDSubiquitination[1]
453GIDLEKIKAYIDSFRubiquitination[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] 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]
 [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] 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]
 [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] 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]
 [7] 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]
 [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
 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
 REGION 411 415 Binding site for the 3'-end of tRNA
 MOD_RES 74 74 N6-acetyllysine.
 MOD_RES 249 249 Phosphoserine.
 MOD_RES 374 374 N6-acetyllysine.
 MOD_RES 500 500 Phosphothreonine; by PKA (Potential).  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 501 AA 
Protein Sequence
MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD LTIQKADEVV 60
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV 120
RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL 180
DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF 240
KNNAYLAQSP QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 300
EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV 360
EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 420
RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF 480
LGLHNVRQTS MFPRDPKRLT P 501 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0004046; F:aminoacylase activity; TAS:ProtInc.
 GO:0004815; F:aspartate-tRNA ligase activity; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0006422; P:aspartyl-tRNA aminoacylation; TAS:ProtInc.
 GO:0006461; P:protein complex assembly; TAS:ProtInc. 
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.