CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023620
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phenylalanine--tRNA ligase alpha subunit 
Protein Synonyms/Alias
 CML33; Phenylalanyl-tRNA synthetase alpha subunit; PheRS 
Gene Name
 FARSA 
Gene Synonyms/Alias
 FARS; FARSL; FARSLA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
59EAELRSTKHWELTAEubiquitination[1, 2, 3, 4]
101LMRLPSGKVGFSKAMubiquitination[1, 2, 3, 5]
106SGKVGFSKAMSNKWIubiquitination[1, 2, 3, 5]
111FSKAMSNKWIRVDKSubiquitination[2, 3]
117NKWIRVDKSAADGPRubiquitination[1, 3]
150VRGGQAEKLGEKERSubiquitination[1, 3]
154QAEKLGEKERSELRKubiquitination[3]
163RSELRKRKLLAEVTLubiquitination[3]
177LKTYWVSKGSAFSTSubiquitination[1, 3, 4]
187AFSTSISKQETELSPubiquitination[1, 2, 3, 4, 5]
208SWRDRPFKPYNFLAHubiquitination[3]
311GYGSQGYKYNWKLDEacetylation[6]
311GYGSQGYKYNWKLDEubiquitination[1, 2, 3, 4, 5]
315QGYKYNWKLDEARKNubiquitination[1, 2, 3, 4, 5, 7]
342ALYRLAQKKPFTPVKubiquitination[3]
343LYRLAQKKPFTPVKYubiquitination[1, 3]
349KKPFTPVKYFSIDRVubiquitination[1, 3, 4, 7]
397VLREFFTKLGITQLRubiquitination[1, 3, 5]
406GITQLRFKPAYNPYTubiquitination[1, 3, 7]
427FSYHQGLKKWVEVGNubiquitination[1, 2, 3, 4]
468LERPTMIKYGINNIRubiquitination[7]
481IRELVGHKVNLQMVYubiquitination[2, 3, 7]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
  
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 193 193 Phosphoserine.
 MOD_RES 311 311 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 508 AA 
Protein Sequence
MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV IEAELRSTKH 60
WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG KVGFSKAMSN KWIRVDKSAA 120
DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK LGEKERSELR KRKLLAEVTL KTYWVSKGSA 180
FSTSISKQET ELSPEMISSG SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE 240
MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH 300
SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY FSIDRVFRNE 360
TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF 420
SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH 480
KVNLQMVYDS PLCRLDAEPR PPPTQEAA 508 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004826; F:phenylalanine-tRNA ligase activity; TAS:ProtInc.
 GO:0000049; F:tRNA binding; IEA:InterPro.
 GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 
Interpro
 IPR006195; aa-tRNA-synth_II.
 IPR004529; Phe-tRNA-synth_IIc_asu.
 IPR002319; Phenylalanyl-tRNA_Synthase.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF01409; tRNA-synt_2d 
SMART
  
PROSITE
 PS50862; AA_TRNA_LIGASE_II 
PRINTS