CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023728
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
 CGI-04 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43QGLLAAQKARGLFKDubiquitination[1]
58FFPETGTKIELPELFubiquitination[1]
281ITSTTGAKLGKSAGNubiquitination[1, 2]
284TTGAKLGKSAGNAVWubiquitination[3]
296AVWLNRDKTSPFELYubiquitination[1, 3]
355RLAAEVTKLVHGREGacetylation[4, 5, 6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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] 
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 82 91 "HIGH" region.
 MOTIF 281 285 "KMSKS" region.
 BINDING 284 284 ATP (By similarity).
 MOD_RES 355 355 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Disease mutation; Ligase; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 477 AA 
Protein Sequence
MAAPILRSFS WGRWSGTLNL SVLLPLGLRK AHSGAQGLLA AQKARGLFKD FFPETGTKIE 60
LPELFDRGTA SFPQTIYCGF DPTADSLHVG HLLALLGLFH LQRAGHNVIA LVGGATARLG 120
DPSGRTKERE ALETERVRAN ARALRLGLEA LAANHQQLFT DGRSWGSFTV LDNSAWYQKQ 180
HLVDFLAAVG GHFRMGTLLS RQSVQLRLKS PEGMSLAEFF YQVLQAYDFY YLFQRYGCRV 240
QLGGSDQLGN IMSGYEFINK LTGEDVFGIT VPLITSTTGA KLGKSAGNAV WLNRDKTSPF 300
ELYQFFVRQP DDSVERYLKL FTFLPLPEID HIMQLHVKEP ERRGPQKRLA AEVTKLVHGR 360
EGLDSAKRCT QALYHSSIDA LEVMSDQELK ELFKEAPFSE FFLDPGTSVL DTCRKANAIP 420
DGPRGYRMIT EGGVSINHQQ VTNPESVLIV GQHILKNGLS LLKIGKRNFY IIKWLQL 477 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0005524; F:ATP binding; TAS:BHF-UCL.
 GO:0000049; F:tRNA binding; IDA:BHF-UCL.
 GO:0072545; F:tyrosine binding; IDA:BHF-UCL.
 GO:0004831; F:tyrosine-tRNA ligase activity; NAS:UniProtKB.
 GO:0070184; P:mitochondrial tyrosyl-tRNA aminoacylation; IMP:BHF-UCL. 
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.