CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036993
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Threonine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
  
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
90ALCKKIIKEKQAFERubiquitination[1]
101AFERLEVKKETLLAMubiquitination[1]
102FERLEVKKETLLAMFubiquitination[1]
110ETLLAMFKYNKFKCRubiquitination[1, 2]
122KCRILNEKVNTPTTTacetylation[3, 4]
122KCRILNEKVNTPTTTubiquitination[1, 2, 4, 5, 6, 7, 8]
158IKALKIHKNSSTYWEubiquitination[1, 2, 6, 7]
167SSTYWEGKADMETLQubiquitination[1, 2, 6, 7, 8]
185GISFPDPKMLKEWEKubiquitination[5, 6]
188FPDPKMLKEWEKFQEubiquitination[1, 4]
192KMLKEWEKFQEEAKNacetylation[9]
192KMLKEWEKFQEEAKNubiquitination[1, 5]
288EKELFALKPMNCPGHubiquitination[1]
383NLSTRPEKFLGDIEVubiquitination[1, 2, 5, 6, 8]
396EVWDQAEKQLENSLNubiquitination[8]
408SLNEFGEKWELNSGDacetylation[3]
408SLNEFGEKWELNSGDubiquitination[1, 2, 6, 8]
422DGAFYGPKIDIQIKDubiquitination[6]
428PKIDIQIKDAIGRYHubiquitination[1, 2, 5, 6, 8]
463SHDGDDKKRPVIVHRubiquitination[2]
490LTENYGGKWPFWLSPubiquitination[2, 8]
515TCDEYAQKVRQQFHDubiquitination[1, 2, 7, 8]
524RQQFHDAKFMADIDLubiquitination[1, 2]
539DPGCTLNKKIRNAQLacetylation[3]
539DPGCTLNKKIRNAQLubiquitination[2, 7]
540PGCTLNKKIRNAQLAubiquitination[1]
560LVVGEKEKISGTVNIubiquitination[1]
591IERLQQLKEFRSKQAacetylation[9]
591IERLQQLKEFRSKQAubiquitination[1, 2, 6, 7, 8]
596QLKEFRSKQAEEEF*ubiquitination[2, 4, 6, 7, 8]
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] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 602 AA 
Protein Sequence
MIPFWQKRQK KIASQLKSLC LMVNRLMRNL GKLHHIKLPV ELAMERVYGG CLCYGPPIEN 60
GFYYDMYLEE GGVSSNDFSS LEALCKKIIK EKQAFERLEV KKETLLAMFK YNKFKCRILN 120
EKVNTPTTTV YRCGPLIDLC RGPHVRHTGK IKALKIHKNS STYWEGKADM ETLQRIYGIS 180
FPDPKMLKEW EKFQEEAKNR DHRKIGRDQE LYFFHELSPG SCFFLPKGAY IYNALIEFIR 240
SEYRKRGFQE VVTPNIFNSR LWMTSGHWQH YSENMFSFEV EKELFALKPM NCPGHCLMFD 300
HRPRSWRELP LRLADFGVLH RNELSGALTG LTRVRRFQQD DAHIFCAMEQ IEDEIKGCLD 360
FLRTVYSVFG FSFKLNLSTR PEKFLGDIEV WDQAEKQLEN SLNEFGEKWE LNSGDGAFYG 420
PKIDIQIKDA IGRYHQCATI QLDFQLPIRF NLTYVSHDGD DKKRPVIVHR AILGSVERMI 480
AILTENYGGK WPFWLSPRQV MVVPVGPTCD EYAQKVRQQF HDAKFMADID LDPGCTLNKK 540
IRNAQLAQYN FILVVGEKEK ISGTVNIRTR DNKVHGERTI SETIERLQQL KEFRSKQAEE 600
EF 602 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0004829; F:threonine-tRNA ligase activity; IEA:InterPro.
 GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR002314; aa-tRNA-synt_IIb_cons-dom.
 IPR006195; aa-tRNA-synth_II.
 IPR004154; Anticodon-bd.
 IPR002320; Thr-tRNA-ligase_IIa.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF03129; HGTP_anticodon
 PF00587; tRNA-synt_2b
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01047; TRNASYNTHTHR.