CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015302
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Aspartyl-tRNA synthetase; AspRS 
Gene Name
 DARS2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
104DESAASVKKILCEAPubiquitination[1, 2]
142PTGEIEIKVKTAELLacetylation[3]
224KRTPGGAKEFLVPSRubiquitination[4, 5]
235VPSREPGKFYSLPQSacetylation[6]
235VPSREPGKFYSLPQSubiquitination[4, 5]
340PDTRFGMKIIDISDVubiquitination[1]
368SKPHGTVKAICIPEGubiquitination[7]
382GAKYLKRKDIESIRNacetylation[6, 8, 9]
454KACSLLGKLRLECADubiquitination[7]
606RDVIAFPKSFRGHDLubiquitination[4, 5]
627SVPPEELKPYHIRVSacetylation[6, 8]
Reference
 [1] 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]
 [2] 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]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] 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 219 219 Phosphothreonine (By similarity).
 MOD_RES 382 382 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Disease mutation; Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 645 AA 
Protein Sequence
MYFPSWLSQL YRGLSRPIRR TTQPIWGSLY RSLLQSSQRR IPEFSSFVVR TNTCGELRSS 60
HLGQEVTLCG WIQYRRQNTF LVLRDFDGLV QVIIPQDESA ASVKKILCEA PVESVVQVSG 120
TVISRPAGQE NPKMPTGEIE IKVKTAELLN ACKKLPFEIK NFVKKTEALR LQYRYLDLRS 180
FQMQYNLRLR SQMVMKMREY LCNLHGFVDI ETPTLFKRTP GGAKEFLVPS REPGKFYSLP 240
QSPQQFKQLL MVGGLDRYFQ VARCYRDEGS RPDRQPEFTQ IDIEMSFVDQ TGIQSLIEGL 300
LQYSWPNDKD PVVVPFPTMT FAEVLATYGT DKPDTRFGMK IIDISDVFRN TEIGFLQDAL 360
SKPHGTVKAI CIPEGAKYLK RKDIESIRNF AADHFNQEIL PVFLNANRNW NSPVANFIME 420
SQRLELIRLM ETQEEDVVLL TAGEHNKACS LLGKLRLECA DLLETRGVVL RDPTLFSFLW 480
VVDFPLFLPK EENPRELESA HHPFTAPHPS DIHLLYTEPK KARSQHYDLV LNGNEIGGGS 540
IRIHNAELQR YILATLLKED VKMLSHLLQA LDYGAPPHGG IALGLDRLIC LVTGSPSIRD 600
VIAFPKSFRG HDLMSNTPDS VPPEELKPYH IRVSKPTDSK AERAH 645 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004815; F:aspartate-tRNA ligase activity; TAS:Reactome.
 GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; TAS:BHF-UCL.
 GO:0000049; F:tRNA binding; TAS:BHF-UCL.
 GO:0070145; P:mitochondrial asparaginyl-tRNA aminoacylation; IC:BHF-UCL. 
Interpro
 IPR004364; aa-tRNA-synt_II.
 IPR018150; aa-tRNA-synt_II-like.
 IPR006195; aa-tRNA-synth_II.
 IPR004524; Asp-tRNA-ligase_IIb_bac/mt.
 IPR002312; Asp/Asn-tRNA-synth_IIb.
 IPR004115; GAD_dom.
 IPR012340; NA-bd_OB-fold.
 IPR004365; NA-bd_OB_tRNA-helicase. 
Pfam
 PF02938; GAD
 PF00152; tRNA-synt_2
 PF01336; tRNA_anti 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01042; TRNASYNTHASP.