CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016660
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Tyrosyl-tRNA synthetase; TyrRS 
Gene Name
 Yars2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
43PRARGLFKEFFPESGacetylation[1]
362QEGLDSAKRCTQALYacetylation[1, 2, 3]
362QEGLDSAKRCTQALYsuccinylation[3]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [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
 Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr) (By similarity). 
Sequence Annotation
 MOTIF 77 86 "HIGH" region.
 MOTIF 276 280 "KMSKS" region.
 BINDING 279 279 ATP (By similarity).
 MOD_RES 350 350 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 472 AA 
Protein Sequence
MAAPMLRRLC RVPQSLVWLR GSRAVRPGAR GMLVAPRARG LFKEFFPESG TKTELPELFD 60
RRRAGSSPQT VYCGFDPTGD SLHVGHLLTL LGLFHFQRAG HNVIALVGGS TALLGDPSGR 120
TKGREALSAE CVRANAHALR RGLEALAANH ARLFADGRPW GSFTVLDNAA WFQEQHLVDF 180
LATVGGHFRM GTLLSRLSVQ SRLKSPEGMS LAEFFYQVLQ AYDFYYLFQH YGCRVQLGGS 240
DQLGNIMSGY EFIHKLTGED VFGITVPLIT STTGAKLGKS AGNAVWLNRE KTSPFELYQF 300
FVRQQDDSVE RYLKLFTFLP LPEIDHIMQL HVKEPEKRVA QKRLAAEVTK LVHGQEGLDS 360
AKRCTQALYH SSIEALEVMS DQELKELFKE ASFSELVLDP GTSVIDTCRK ANAIPDGPRG 420
YRMITEGGVS INHRQVTNPE SVLVIGQHIL KNGLSLLKIG KRNFYIIKWL QL 472 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0072545; F:tyrosine binding; IEA:Compara.
 GO:0004831; F:tyrosine-tRNA ligase activity; IEA:EC.
 GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002305; aa-tRNA-synth_Ic.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR002942; S4_RNA-bd.
 IPR002307; Tyr-tRNA-ligase.
 IPR024088; Tyr-tRNA-ligase_bac-type. 
Pfam
 PF00579; tRNA-synt_1b 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR01040; TRNASYNTHTYR.