CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004100
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Glutamine--tRNA ligase 
Protein Synonyms/Alias
 Glutaminyl-tRNA synthetase; GlnRS 
Gene Name
 GLN4 
Gene Synonyms/Alias
 YOR168W; O3601 
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
28VKEIVKNKKVSDSLYacetylation[1]
29KEIVKNKKVSDSLYKacetylation[1]
63HNLASFVKGTDLPKSacetylation[2]
153PGIFADVKNLKELKWacetylation[2]
167WADPRSFKPIIDQEVacetylation[2]
297FDDTNPEKEAPEYFEacetylation[2]
316MVSWLGFKPWKITYSubiquitination[3]
339RLAEVLIKNGKAYVCacetylation[2]
404GEAILRMKQDLNSPSubiquitination[3]
508IAQLVDEKFVRGWDDacetylation[2]
628FSENVDDKEFFRLTPacetylation[2]
671IHVNYDNKVEEGSKPacetylation[2]
724SHPEGFLKDINPESEacetylation[2]
Reference
 [1] Preparative peptide isoelectric focusing as a tool for improving the identification of lysine-acetylated peptides from complex mixtures.
 Xie H, Bandhakavi S, Roe MR, Griffin TJ.
 J Proteome Res. 2007 May;6(5):2019-26. [PMID: 17397211]
 [2] 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]
 [3] 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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 MOTIF 258 268 "HIGH" region.
 MOTIF 495 499 "KMSKS" region.
 BINDING 498 498 ATP (By similarity).
 MOD_RES 378 378 Phosphoserine.  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 809 AA 
Protein Sequence
MSSVEELTQL FSQVGFEDKK VKEIVKNKKV SDSLYKLIKE TPSDYQWNKS TRALVHNLAS 60
FVKGTDLPKS ELIVNGIING DLKTSLQVDA AFKYVKANGE ASTKMGMNEN SGVGIEITED 120
QVRNYVMQYI QENKERILTE RYKLVPGIFA DVKNLKELKW ADPRSFKPII DQEVLKLLGP 180
KDERDLIKKK TKNNEKKKTN SAKKSSDNSA SSGPKRTMFN EGFLGDLHKV GENPQAYPEL 240
MKEHLEVTGG KVRTRFPPEP NGYLHIGHSK AIMVNFGYAK YHNGTCYLRF DDTNPEKEAP 300
EYFESIKRMV SWLGFKPWKI TYSSDYFDEL YRLAEVLIKN GKAYVCHCTA EEIKRGRGIK 360
EDGTPGGERY ACKHRDQSIE QNLQEFRDMR DGKYKPGEAI LRMKQDLNSP SPQMWDLIAY 420
RVLNAPHPRT GTKWRIYPTY DFTHCLVDSM ENITHSLCTT EFYLSRESYE WLCDQVHVFR 480
PAQREYGRLN ITGTVLSKRK IAQLVDEKFV RGWDDPRLFT LEAIRRRGVP PGAILSFINT 540
LGVTTSTTNI QVVRFESAVR KYLEDTTPRL MFVLDPVEVV VDNLSDDYEE LATIPYRPGT 600
PEFGERTVPF TNKFYIERSD FSENVDDKEF FRLTPNQPVG LIKVSHTVSF KSLEKDEAGK 660
IIRIHVNYDN KVEEGSKPKK PKTYIQWVPI SSKYNSPLRV TETRVYNQLF KSENPSSHPE 720
GFLKDINPES EVVYKESVME HNFGDVVKNS PWVVDSVKNS EFYVEEDKDS KEVCRFQAMR 780
VGYFTLDKES TTSKVILNRI VSLKDATSK 809 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004819; F:glutamine-tRNA ligase activity; IDA:SGD.
 GO:0006425; P:glutaminyl-tRNA aminoacylation; IMP:SGD. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR004514; Gln-tRNA-synth_Ib.
 IPR007638; Gln-tRNA-synth_Ib_RNA-bd_2.
 IPR007639; Gln-tRNA-synth_Ib_RNA-bd_N.
 IPR000924; Glu/Gln-tRNA-synth_Ib.
 IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
 IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
 IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
 IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl.
 IPR011035; Ribosomal_L25/Gln-tRNA_synth.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00749; tRNA-synt_1c
 PF03950; tRNA-synt_1c_C
 PF04558; tRNA_synt_1c_R1
 PF04557; tRNA_synt_1c_R2 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00987; TRNASYNTHGLU.