CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023509
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
 Farsb 
Gene Synonyms/Alias
 Farsl; Farslb; Frsb 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
53SKEQGHGKAQGASDVubiquitination[1]
64ASDVVLYKIDVPANRacetylation[2]
133LRNIKFTKDRYDSFIacetylation[3]
190FKPLNKTKEYTACELacetylation[4]
262CTGTDFTKAKIVLDIacetylation[4]
443AVHISNPKTAEFQVAubiquitination[1]
467KTIAANRKMPLPLKLubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
  
Sequence Annotation
 DOMAIN 302 379 B5.  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 589 AA 
Protein Sequence
MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKQIISKEQG HGKAQGASDV 60
VLYKIDVPAN RYDLLCLEGL ARGLQVFKER IKAPVYKRVM PKGDIQKLVI TEETAKVRPF 120
AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI CRKRALVAIG THDLDTLSGP FTYTAKRPSD 180
IKFKPLNKTK EYTACELMNI YKTDNHLKHY LHIIESKPLY PVIYDSNGVV LSMPPIINGN 240
HSKITVNTRN IFIECTGTDF TKAKIVLDII VTMFSEHCEN QFTVEAVEVV SPNGKSSTFP 300
ELPYRKEMVR ADLINKKVGI RETPANLAKL LTRMCLKSEV IGDGNQIEVE IPPTRADVIH 360
ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL RLDMAAAGFT EALTFALCSQ 420
EDIADKLGLD ISATKAVHIS NPKTAEFQVA RTTLLPGLLK TIAANRKMPL PLKLFEISDV 480
VVKDSGKDVG AKNYRHLCAV YYNKTPGFEI IHGLLDRIMQ LLDVPPGEES GGYMIKASAG 540
SAFFPGRCAE IFVGGQSIGK LGVLHPDVIT KFELTMPCSS LEINIEPFL 589 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 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; IEA:InterPro. 
Interpro
 IPR005146; B3/B4_tRNA-bd.
 IPR009061; DNA-bd_dom_put.
 IPR004531; Phe-tRNA-synth_IIc_bsu_arc.
 IPR020825; Phe-tRNA_synthase_B3/B4.
 IPR005147; tRNA_synthase_B5-dom. 
Pfam
 PF03483; B3_4
 PF03484; B5 
SMART
 SM00873; B3_4
 SM00874; B5 
PROSITE
 PS51483; B5 
PRINTS