CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020269
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Threonine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Threonyl-tRNA synthetase; ThrRS; Threonyl-tRNA synthetase-like 1 
Gene Name
 TARS2 
Gene Synonyms/Alias
 TARSL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
70ISLPGGQKIDAVAWNubiquitination[1]
169YHDFFLGKERTIRGSubiquitination[1, 2]
210DQLRQLFKDNPFKLHubiquitination[1]
215LFKDNPFKLHLIEEKubiquitination[1, 2]
352HRGFSEVKTPTLFSTubiquitination[1]
405ITDTLALKPMNCPAHubiquitination[1]
572LRFDLQYKGQAGALEubiquitination[1, 2]
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] 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] 
Functional Description
  
Sequence Annotation
 MOD_RES 52 52 Phosphoserine.  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 718 AA 
Protein Sequence
MALYQRWRCL RLQGLQACRL HTAVVSTPPR WLAERLGLFE ELWAAQVKRL ASMAQKEPRT 60
IKISLPGGQK IDAVAWNTTP YQLARQISST LADTAVAAQV NGEPYDLERP LETDSDLRFL 120
TFDSPEGKAV FWHSSTHVLG AAAEQFLGAV LCRGPSTEYG FYHDFFLGKE RTIRGSELPV 180
LERICQELTA AARPFRRLEA SRDQLRQLFK DNPFKLHLIE EKVTGPTATV YGCGTLVDLC 240
QGPHLRHTGQ IGGLKLLSNS SSLWRSSGAP ETLQRVSGIS FPTTELLRVW EAWREEAELR 300
DHRRIGKEQE LFFFHELSPG SCFFLPRGTR VYNALVAFIR AEYAHRGFSE VKTPTLFSTK 360
LWEQSGHWEH YQEDMFAVQP PGSDRPPSSQ SDDSTRHITD TLALKPMNCP AHCLMFAHRP 420
RSWRELPLRL ADFGALHRAE ASGGLGGLTR LRCFQQDDAH IFCTTDQLEA EIQSCLDFLR 480
SVYAVLGFSF RLALSTRPSG FLGDPCLWDQ AEQVLKQALK EFGEPWDLNS GDGAFYGPKI 540
DVHLHDALGR PHQCGTIQLD FQLPLRFDLQ YKGQAGALER PVLIHRAVLG SVERLLGVLA 600
ESCGGKWPLW LSPFQVVVIP VGSEQEEYAK EAQQSLRAAG LVSDLDADSG LTLSRRIRRA 660
QLAHYNFQFV VGQKEQSKRT VNIRTRDNRR LGEWDLPEAV QRLVELQNTR VPNAEEIF 718 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004829; F:threonine-tRNA ligase activity; IEA:EC.
 GO:0070159; P:mitochondrial threonyl-tRNA aminoacylation; TAS:BHF-UCL. 
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.