CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005168
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tryptophan--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Interferon-induced protein 53; IFP53; Tryptophanyl-tRNA synthetase; TrpRS; hWRS; T1-TrpRS; T2-TrpRS 
Gene Name
 WARS 
Gene Synonyms/Alias
 IFI53; WRS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27GELVRSLKAGNASKDubiquitination[1, 2]
33LKAGNASKDEIDSAVubiquitination[1]
47VKMLVSLKMSYKAAAubiquitination[1]
51VSLKMSYKAAAGEDYubiquitination[1]
102AKGIDYDKLIVRFGSubiquitination[1, 2, 3, 4, 5]
111IVRFGSSKIDKELINubiquitination[2]
114FGSSKIDKELINRIEubiquitination[2]
153VLDAYENKKPFYLYTubiquitination[2]
154LDAYENKKPFYLYTGubiquitination[2, 3, 5]
366IFLTDTAKQIKTKVNacetylation[6]
366IFLTDTAKQIKTKVNubiquitination[1, 2]
369TDTAKQIKTKVNKHAubiquitination[2]
431AMLTGELKKALIEVLubiquitination[1]
432MLTGELKKALIEVLQubiquitination[2]
450AEHQARRKEVTDEIVubiquitination[7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [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] 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]
 [7] 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
Functional Description
 Isoform 1, isoform 2 and T1-TrpRS have aminoacylation activity while T2-TrpRS lacks it. Isoform 2, T1-TrpRS and T2-TrpRS possess angiostatic activity whereas isoform 1 lacks it. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression. 
Sequence Annotation
 DOMAIN 8 64 WHEP-TRS.
 MOTIF 164 173 "HIGH" region.
 MOTIF 349 353 "KMSKS" region.  
Keyword
 3D-structure; Alternative splicing; Aminoacyl-tRNA synthetase; Angiogenesis; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 471 AA 
Protein Sequence
MPNSEPASLL ELFNSIATQG ELVRSLKAGN ASKDEIDSAV KMLVSLKMSY KAAAGEDYKA 60
DCPPGNPAPT SNHGPDATEA EEDFVDPWTV QTSSAKGIDY DKLIVRFGSS KIDKELINRI 120
ERATGQRPHH FLRRGIFFSH RDMNQVLDAY ENKKPFYLYT GRGPSSEAMH VGHLIPFIFT 180
KWLQDVFNVP LVIQMTDDEK YLWKDLTLDQ AYSYAVENAK DIIACGFDIN KTFIFSDLDY 240
MGMSSGFYKN VVKIQKHVTF NQVKGIFGFT DSDCIGKISF PAIQAAPSFS NSFPQIFRDR 300
TDIQCLIPCA IDQDPYFRMT RDVAPRIGYP KPALLHSTFF PALQGAQTKM SASDPNSSIF 360
LTDTAKQIKT KVNKHAFSGG RDTIEEHRQF GGNCDVDVSF MYLTFFLEDD DKLEQIRKDY 420
TSGAMLTGEL KKALIEVLQP LIAEHQARRK EVTDEIVKEF MTPRKLSFDF Q 471 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004830; F:tryptophan-tRNA ligase activity; NAS:UniProtKB.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
 GO:0006436; P:tryptophanyl-tRNA aminoacylation; NAS:UniProtKB. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002305; aa-tRNA-synth_Ic.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009068; S15_NS1_RNA-bd.
 IPR002306; Trp-tRNA-ligase.
 IPR000738; WHEP-TRS. 
Pfam
 PF00579; tRNA-synt_1b
 PF00458; WHEP-TRS 
SMART
 SM00991; WHEP-TRS 
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS00762; WHEP_TRS_1
 PS51185; WHEP_TRS_2 
PRINTS
 PR01039; TRNASYNTHTRP.