CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006256
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tryptophan--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Tryptophanyl-tRNA synthetase; TrpRS; T1-TrpRS; T2-TrpRS 
Gene Name
 Wars 
Gene Synonyms/Alias
 Wrs 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
63AAMGEEYKAGCPPGNacetylation[1]
106AKGIDYDKLIVQFGSubiquitination[2]
158LDAYENKKPFYLYTGacetylation[3]
158LDAYENKKPFYLYTGsuccinylation[3]
158LDAYENKKPFYLYTGubiquitination[2]
260RNVVKIQKHVTFNQVacetylation[1]
370IFLTDTAKQIKSKVNubiquitination[2]
436MLTGELKKTLIDVLQubiquitination[2]
454AEHQARRKAVTEETVubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
 T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it. T1-TrpRS and T2-TrpRS possess angiostatic activity. 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 (By similarity). 
Sequence Annotation
 DOMAIN 12 68 WHEP-TRS.
 MOTIF 168 177 "HIGH" region.
 MOTIF 353 357 "KMSKS" region.  
Keyword
 Alternative splicing; Aminoacyl-tRNA synthetase; Angiogenesis; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 481 AA 
Protein Sequence
MADMPSGESC TSPLELFNSI ATQGELVRSL KAGNAPKDEI DSAVKMLLSL KMSYKAAMGE 60
EYKAGCPPGN PTAGRNCDSD ATKASEDFVD PWTVRTSSAK GIDYDKLIVQ FGSSKIDKEL 120
INRIERATGQ RPHRFLRRGI FFSHRDMNQI LDAYENKKPF YLYTGRGPSS EAMHLGHLVP 180
FIFTKWLQDV FNVPLVIQMS DDEKYLWKDL TLEQAYSYTV ENAKDIIACG FDINKTFIFS 240
DLEYMGQSPG FYRNVVKIQK HVTFNQVKGI FGFTDSDCIG KISFPAVQAA PSFSNSFPKI 300
FRDRTDIQCL IPCAIDQDPY FRMTRDVAPR IGHPKPALLH STFFPALQGA QTKMSASDPN 360
SSIFLTDTAK QIKSKVNKHA FSGGRDTVEE HRQFGGNCEV DVSFMYLTFF LEDDDRLEQI 420
RKDYTSGAML TGELKKTLID VLQPLIAEHQ ARRKAVTEET VKEFMTPRQL SFHFQCFCFD 480
T 481 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004830; F:tryptophan-tRNA ligase activity; IEA:EC.
 GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
 GO:0045765; P:regulation of angiogenesis; IEA:Compara.
 GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:InterPro. 
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.