CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020741
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
62TRLDMYNKLKAEHDSubiquitination[1]
90KVTLPDGKQVDAESWacetylation[2]
230ETLLEMFKYNKFKCRacetylation[3]
230ETLLEMFKYNKFKCRubiquitination[1]
242KCRILNEKVNTPTTTacetylation[2, 3, 4]
242KCRILNEKVNTPTTTubiquitination[1]
278IKTLKIHKNSSTYWEacetylation[3]
278IKTLKIHKNSSTYWEubiquitination[1]
287SSTYWEGKADMETLQubiquitination[1]
305GISFPDPKLLKEWEKubiquitination[1]
308FPDPKLLKEWEKFQEubiquitination[1]
548PKIDIQIKDAIGRYHacetylation[2]
635TCDEYAQKVRQQFHDubiquitination[1]
644RQQFHDAKFMADTDLacetylation[2, 3, 4, 5]
659DPGCTLNKKIRNAQLacetylation[3, 5]
711VRRLQQLKQTRSKQAacetylation[3]
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]
 [4] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654
Functional Description
  
Sequence Annotation
 MOD_RES 242 242 N6-acetyllysine (By similarity).
 MOD_RES 297 297 Phosphotyrosine.
 CROSSLNK 221 221 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Isopeptide bond; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 722 AA 
Protein Sequence
MSQEKASSPS GKMDGEKPVD ASEEKRKEGG KKKSKDGGGD GGRAELNPWP EYINTRLDMY 60
NKLKAEHDSI LAEKAAKDSK PIKVTLPDGK QVDAESWKTT PYQIACGISQ GLADNTVVAK 120
VNKVVWDLDR PLETDCTLEL LKFEDEEAQA VYWHSSAHIM GEAMERVYGG CLCYGPPIEN 180
GFYYDMYLEE GGVSSNDFSS LETLCKKIIK EKQTFERLEV KKETLLEMFK YNKFKCRILN 240
EKVNTPTTTV YRCGPLIDLC RGPHVRHTGK IKTLKIHKNS STYWEGKADM ETLQRIYGIS 300
FPDPKLLKEW EKFQEEAKNR DHRKIGRDQE LYFFHELSPG SCFFLPKGAY IYNTLMEFIR 360
SEYRKRGFQE VVTPNIFNSR LWMTSGHWQH YSENMFSFEV EKEQFALKPM NCPGHCLMFD 420
HRPRSWRELP LRLADFGVLH RNELSGALTG LTRVRRFQQD DAHIFCAMEQ IEDEIKGCLD 480
FLRTVYSVFG FSFKLNLSTR PEKFLGDIEI WNQAEKQLEN SLNEFGEKWE LNPGDGAFYG 540
PKIDIQIKDA IGRYHQCATI QLDFQLPIRF NLTYVSHDGD DKKRPVIVHR AILGSVERMI 600
AILTENYGGK WPFWLSPRQV MVVPVGPTCD EYAQKVRQQF HDAKFMADTD LDPGCTLNKK 660
IRNAQLAQYN FILVVGEKEK ASGTVNIRTR DNKVHGERTV EETVRRLQQL KQTRSKQAEE 720
EF 722 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004829; F:threonine-tRNA ligase activity; IEA:EC.
 GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro. 
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.