CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006981
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative proline--tRNA ligase YHR020W 
Protein Synonyms/Alias
 Prolyl-tRNA synthetase; ProRS 
Gene Name
 YHR020W 
Gene Synonyms/Alias
  
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
15AKLCVNEKPPAESAVubiquitination[1]
140NNFEDSQKVVDFSQEacetylation[2]
150DFSQEVSKETATEGKubiquitination[1]
314SYRDLPLKLNQWNSVacetylation[2]
314SYRDLPLKLNQWNSVubiquitination[1]
327SVVRWEFKHPQPFLRacetylation[2]
386GRKTEKEKFAGGDFTubiquitination[1]
485VIPVGITKKTSEEQRacetylation[2]
533KFSQYELKGIPIRIEacetylation[2]
544IRIELGPKDIEKNQVacetylation[2]
548LGPKDIEKNQVVVVRacetylation[2]
647EEFEEDDKAPSMGAKacetylation[2]
Reference
 [1] 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]
 [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] 
Functional Description
  
Sequence Annotation
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 170 170 Phosphothreonine.
 MOD_RES 655 655 Phosphoserine.  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 688 AA 
Protein Sequence
MPVSEAFAKL CVNEKPPAES AVAVKSLVFK PKTPKSATPV PIVVVALQST TTPSALIANA 60
TSSKDPRLAR DDLVKQAFQS ESARAFILGD LANATSNFHL LIDHELGTVD GDTILQLNDS 120
TYMKKSDMMK FLNNFEDSQK VVDFSQEVSK ETATEGKKQQ KKQQPSKAGT AAAAAAAALE 180
DAKLIGITVD KALDFPGWYQ QILTKGEMLD YYDVSGCYIL RPPSYAIWEN IQKWFDDKIK 240
AIGVQNAYFP MFVSSRVLEK EKDHVEGFAP EVAWVTRAGS SELEEPIAIR PTSETVMYPY 300
YAKWVQSYRD LPLKLNQWNS VVRWEFKHPQ PFLRTREFLW QEGHTAHLTA KDAEEEVLQI 360
LDFYAGVYEE LLAVPVVKGR KTEKEKFAGG DFTTTCEGYI PQTGRGIQGA TSHHLGQNFS 420
KMFNLSVENP LGSDHPKIFA YQNSWGLSTR VIGVMVMIHS DNKGLVIPPR VSQFQSVVIP 480
VGITKKTSEE QRKHIHETAR SVESRLKKVG IRAFGDYNDN YTPGWKFSQY ELKGIPIRIE 540
LGPKDIEKNQ VVVVRRNDSK KYVVSFDELE ARIPEILEEM QGDLFKKAKE LFDTHRVIVN 600
EWSGFVPALN KKNVILAPWC GVMECEEDIK ESSAKKDDGE EFEEDDKAPS MGAKSLCIPF 660
DQPVLNEGQK CIKCERIAVN YCMFGRSY 688 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004827; F:proline-tRNA ligase activity; IDA:SGD.
 GO:0006433; P:prolyl-tRNA aminoacylation; IDA:SGD.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC. 
Interpro
 IPR002314; aa-tRNA-synt_IIb_cons-dom.
 IPR006195; aa-tRNA-synth_II.
 IPR004154; Anticodon-bd.
 IPR002316; Pro-tRNA-ligase_IIa.
 IPR004499; Pro-tRNA-ligase_IIa_arc-type.
 IPR016061; Pro-tRNA_ligase_II_C.
 IPR017449; Pro-tRNA_synth_II.
 IPR007214; YbaK/aa-tRNA-synth-assoc-dom. 
Pfam
 PF03129; HGTP_anticodon
 PF09180; ProRS-C_1
 PF00587; tRNA-synt_2b 
SMART
 SM00946; ProRS-C_1 
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS
 PR01046; TRNASYNTHPRO.