CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005525
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Threonyl-tRNA synthetase; ThrRS 
Gene Name
 TARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MFEEKASSPSGKubiquitination[1]
12KASSPSGKMGGEEKPubiquitination[1]
18GKMGGEEKPIGAGEEubiquitination[1]
26PIGAGEEKQKEGGKKubiquitination[1]
65LEMYNILKAEHDSILubiquitination[1, 2]
75HDSILAEKAEKDSKPubiquitination[1, 2, 3, 4]
91KVTLPDGKQVDAESWubiquitination[1, 2]
99QVDAESWKTTPYQIAubiquitination[1]
211ALCKKIIKEKQAFERubiquitination[1]
213CKKIIKEKQAFERLEubiquitination[1]
222AFERLEVKKETLLAMubiquitination[1, 5]
223FERLEVKKETLLAMFubiquitination[1]
231ETLLAMFKYNKFKCRubiquitination[1, 6]
243KCRILNEKVNTPTTTacetylation[7]
243KCRILNEKVNTPTTTubiquitination[1, 2, 3, 4, 5, 6, 8, 9]
279IKALKIHKNSSTYWEubiquitination[1, 2, 3, 9]
288SSTYWEGKADMETLQubiquitination[1, 2, 3, 4, 9]
306GISFPDPKMLKEWEKacetylation[7]
306GISFPDPKMLKEWEKubiquitination[2, 5, 8]
309FPDPKMLKEWEKFQEubiquitination[1]
313KMLKEWEKFQEEAKNubiquitination[1, 5, 8]
319EKFQEEAKNRDHRKIubiquitination[2]
409EKELFALKPMNCPGHubiquitination[1]
504NLSTRPEKFLGDIEVubiquitination[1, 2, 4, 5, 6, 8]
517EVWDQAEKQLENSLNubiquitination[4]
529SLNEFGEKWELNSGDubiquitination[1, 2, 3, 4]
543DGAFYGPKIDIQIKDubiquitination[2]
549PKIDIQIKDAIGRYHubiquitination[1, 2, 3, 4, 5, 6, 8]
611LTENYGGKWPFWLSPubiquitination[3, 4]
636TCDEYAQKVRQQFHDubiquitination[1, 3, 4, 6, 9]
645RQQFHDAKFMADIDLubiquitination[1]
660DPGCTLNKKIRNAQLubiquitination[9]
661PGCTLNKKIRNAQLAubiquitination[1]
681LVVGEKEKISGTVNIubiquitination[1]
712IERLQQLKEFRSKQAubiquitination[1, 2, 3, 4, 6, 9]
717QLKEFRSKQAEEEF*ubiquitination[2, 3, 4, 9]
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] 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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
  
Sequence Annotation
 MOD_RES 243 243 N6-acetyllysine.
 MOD_RES 298 298 Phosphotyrosine (By similarity).
 CROSSLNK 222 222 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Isopeptide bond; Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 723 AA 
Protein Sequence
MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM 60
YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA 120
KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE 180
NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL 240
NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI 300
SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP GSCFFLPKGA YIYNALIEFI 360
RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF 420
DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL 480
DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY 540
GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM 600
IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK 660
KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE 720
EEF 723 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:HPA.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
 GO:0004829; F:threonine-tRNA ligase activity; NAS:UniProtKB.
 GO:0006435; P:threonyl-tRNA aminoacylation; NAS:UniProtKB. 
Interpro
 IPR002314; aa-tRNA-synt_IIb_cons-dom.
 IPR006195; aa-tRNA-synth_II.
 IPR004154; Anticodon-bd.
 IPR012675; Beta-grasp_dom.
 IPR004095; TGS.
 IPR012676; TGS-like.
 IPR002320; Thr-tRNA-ligase_IIa.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF03129; HGTP_anticodon
 PF02824; TGS
 PF00587; tRNA-synt_2b
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01047; TRNASYNTHTHR.