CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006638
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tyrosine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Tyrosyl-tRNA synthetase; TyrRS 
Gene Name
 TYS1 
Gene Synonyms/Alias
 MGM104; YGR185C; G7522 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
99EVVNYRAKYYELTIKacetylation[1]
118SINVPIEKLKFVVGSacetylation[1]
150IVSQNDAKRAGADVVubiquitination[2]
194FGGVDQRKIFVLAEEubiquitination[2]
236SASDPNSKIDLLEEPacetylation[1]
244IDLLEEPKQVKKKINacetylation[1]
295FFIDRPEKFGGPITYubiquitination[2]
303FGGPITYKSFEEMKLacetylation[1]
313EEMKLAFKEEKLSPPubiquitination[2]
353EFQEASEKGYPVATPacetylation[1]
353EFQEASEKGYPVATPubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
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). The specificity determinants on tRNA(Tyr) are the base pair C1-G72, the discriminator residue A73, and the three anticodon bases G34, U35 and A36. Also involved in nuclear tRNA export. 
Sequence Annotation
 MOTIF 48 56 "HIGH" region.
 MOTIF 227 231 "KMSKS" region.
 MOTIF 360 378 Nuclear localization signal.
 BINDING 43 43 Tyrosine (By similarity).
 BINDING 170 170 Tyrosine (By similarity).
 BINDING 174 174 Tyrosine (By similarity).
 BINDING 177 177 Tyrosine (By similarity).
 BINDING 192 192 Tyrosine (By similarity).
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 235 235 Phosphoserine.
 MOD_RES 359 359 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 394 AA 
Protein Sequence
MSSAATVDPN EAFGLITKNL QEVLNPQIIK DVLEVQKRHL KLYWGTAPTG RPHCGYFVPM 60
TKLADFLKAG CEVTVLLADL HAFLDNMKAP LEVVNYRAKY YELTIKAILR SINVPIEKLK 120
FVVGSSYQLT PDYTMDIFRL SNIVSQNDAK RAGADVVKQV ANPLLSGLIY PLMQALDEQF 180
LDVDCQFGGV DQRKIFVLAE ENLPSLGYKK RAHLMNPMVP GLAQGGKMSA SDPNSKIDLL 240
EEPKQVKKKI NSAFCSPGNV EENGLLSFVQ YVIAPIQELK FGTNHFEFFI DRPEKFGGPI 300
TYKSFEEMKL AFKEEKLSPP DLKIGVADAI NELLEPIRQE FANNKEFQEA SEKGYPVATP 360
QKSKKAKKPK NKGTKYPGAT KTNEIATKLE ETKL 394 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:SGD.
 GO:0005634; C:nucleus; IMP:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004831; F:tyrosine-tRNA ligase activity; IDA:SGD.
 GO:0006437; P:tyrosyl-tRNA aminoacylation; IDA:SGD. 
Interpro
 IPR002305; aa-tRNA-synth_Ic.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR002307; Tyr-tRNA-ligase.
 IPR023617; Tyr-tRNA-ligase_arc/euk-type. 
Pfam
 PF00579; tRNA-synt_1b 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR01040; TRNASYNTHTYR.