CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004355
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phenylalanine--tRNA ligase beta subunit 
Protein Synonyms/Alias
 Phenylalanyl-tRNA synthetase beta subunit; PheRS 
Gene Name
 FRS1 
Gene Synonyms/Alias
 YLR060W; L2165 
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
168ALPPKDIKFVPLNQTacetylation[1]
188DKLIEFYKSPEQKNNacetylation[1]
193FYKSPEQKNNIGRYVubiquitination[2]
216FPVIMDSKDRVCSLPubiquitination[2]
373NNLPKGEKLSNANFIubiquitination[2]
382SNANFIAKPLPINKVacetylation[1]
382SNANFIAKPLPINKVubiquitination[2]
388AKPLPINKVSDIFRVubiquitination[2]
431DNGDLAVKLANPKTLubiquitination[2]
436AVKLANPKTLEYQVVubiquitination[2]
453TLLPGILKTVKENRKacetylation[1]
453TLLPGILKTVKENRKubiquitination[2]
550YFPGRGAKVMFRSKEubiquitination[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, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 DOMAIN 292 370 B5.
 REGION 86 90 CCA binding of tRNA (Potential).  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 595 AA 
Protein Sequence
MPTVSVNKQQ LFDLLGKNYT SQEFDELCFE FGMEMDEDTT EEALKTGEEP ELKLDISANR 60
YDLLCIEGIS QSLNEYLERK ERPDYKLSKP TTKLIIDKST EQIRPFATAA VLRNIKLNEK 120
SYASFIALQD KLHANLCRNR SLVAMGTHDL DSIEGPFHYR ALPPKDIKFV PLNQTQEFTG 180
DKLIEFYKSP EQKNNIGRYV HIIEDSPVFP VIMDSKDRVC SLPPLINSEH SKISVNTRNI 240
LIDITATDKT KAEIVLNILT TMFSRYCDEP FTVEPVEIVS EHNGQSRLAP NFNDRIMDVS 300
IKYINSCLGL DQSADEIAHC LKKMSLHAVQ SKEDKDILHV DIPVTRPDIL HACDIMEDAA 360
VGYGFNNLPK GEKLSNANFI AKPLPINKVS DIFRVASSQA TWVEVLPLTL CSHDENFKFL 420
RQSDNGDLAV KLANPKTLEY QVVRTTLLPG ILKTVKENRK HSLPIKVFET GDVVFKDDKL 480
ERKAYNERHW AAIYVGKNSG FEIIQGLLGK IMQTFRTEWI ADYGAAASGR GYWIEEDDSV 540
KTYFPGRGAK VMFRSKEGAE PKQIGHLGVL HPEVMMNFDV PFAASFVEVN AEVFL 595 
Gene Ontology
 GO:0009328; C:phenylalanine-tRNA ligase complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:EC.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:SGD. 
Interpro
 IPR005146; B3/B4_tRNA-bd.
 IPR009061; DNA-bd_dom_put.
 IPR004531; Phe-tRNA-synth_IIc_bsu_arc.
 IPR005147; tRNA_synthase_B5-dom. 
Pfam
 PF03483; B3_4
 PF03484; B5 
SMART
 SM00873; B3_4
 SM00874; B5 
PROSITE
 PS51483; B5 
PRINTS