CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002161
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Aspartate--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Aspartyl-tRNA synthetase; AspRS 
Gene Name
 DPS1 
Gene Synonyms/Alias
 APS; APS1; YLL018C; L1295 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
27VILGEDGKPLSKKALacetylation[1]
27VILGEDGKPLSKKALubiquitination[2]
72AAAEDTAKDNYGKLPacetylation[1]
77TAKDNYGKLPLIQSRacetylation[1]
95RTGQKRVKFVDLDEAacetylation[1]
103FVDLDEAKDSDKEVLacetylation[1]
107DEAKDSDKEVLFRARacetylation[1]
142SLIQGLVKANKEGTIacetylation[1]
151NKEGTISKNMVKWAGacetylation[1]
266REYLATKKFTEVHTPubiquitination[2]
306AQSPQFNKQQLIVADubiquitination[2]
403KMVRLTYKEGIEMLRubiquitination[2]
414EMLRAAGKEIGDFEDacetylation[1]
414EMLRAAGKEIGDFEDubiquitination[2]
428DLSTENEKFLGKLVRacetylation[1]
437LGKLVRDKYDTDFYIacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 301 301 Phosphoserine.
 MOD_RES 502 502 Phosphoserine.
 MOD_RES 546 546 Phosphoserine.  
Keyword
 3D-structure; 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
 557 AA 
Protein Sequence
MSQDENIVKA VEESAEPAQV ILGEDGKPLS KKALKKLQKE QEKQRKKEER ALQLEAEREA 60
REKKAAAEDT AKDNYGKLPL IQSRDSDRTG QKRVKFVDLD EAKDSDKEVL FRARVHNTRQ 120
QGATLAFLTL RQQASLIQGL VKANKEGTIS KNMVKWAGSL NLESIVLVRG IVKKVDEPIK 180
SATVQNLEIH ITKIYTISET PEALPILLED ASRSEAEAEA AGLPVVNLDT RLDYRVIDLR 240
TVTNQAIFRI QAGVCELFRE YLATKKFTEV HTPKLLGAPS EGGSSVFEVT YFKGKAYLAQ 300
SPQFNKQQLI VADFERVYEI GPVFRAENSN THRHMTEFTG LDMEMAFEEH YHEVLDTLSE 360
LFVFIFSELP KRFAHEIELV RKQYPVEEFK LPKDGKMVRL TYKEGIEMLR AAGKEIGDFE 420
DLSTENEKFL GKLVRDKYDT DFYILDKFPL EIRPFYTMPD PANPKYSNSY DFFMRGEEIL 480
SGAQRIHDHA LLQERMKAHG LSPEDPGLKD YCDGFSYGCP PHAGGGIGLE RVVMFYLDLK 540
NIRRASLFPR DPKRLRP 557 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0004815; F:aspartate-tRNA ligase activity; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IDA:SGD.
 GO:0006422; P:aspartyl-tRNA aminoacylation; IDA:SGD. 
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.