CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029721
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Valine--tRNA ligase 
Protein Synonyms/Alias
  
Gene Name
 VARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
289LPTPPGEKKDVSGPMubiquitination[1, 2]
320WEQQGFFKPEYGRPNacetylation[3]
320WEQQGFFKPEYGRPNubiquitination[1, 4, 5]
418AFLQEVWKWKEEKGDubiquitination[6, 7]
432DRIYHQLKKLGSSLDubiquitination[1, 5]
433RIYHQLKKLGSSLDWubiquitination[1, 5, 8]
450ACFTMDPKLSAAVTEubiquitination[5]
492ISDIEVDKKELTGRTubiquitination[5]
493SDIEVDKKELTGRTLubiquitination[4, 5]
507LLSVPGYKEKVEFGVubiquitination[1]
509SVPGYKEKVEFGVLVubiquitination[5]
552VAVAVHPKDTRYQHLubiquitination[5]
562RYQHLKGKNVIHPFLubiquitination[5]
638LPRFEARKAVLVALKubiquitination[5]
645KAVLVALKERGLFRGubiquitination[5]
667VPLCNRSKDVVEPLLubiquitination[5]
769EAREKAAKEFGVSPDubiquitination[1, 6, 7, 8, 9, 10]
952GYRHFCNKLWNATKFubiquitination[5, 6, 7, 10, 11]
958NKLWNATKFALRGLGacetylation[12]
958NKLWNATKFALRGLGubiquitination[5]
966FALRGLGKGFVPSPTubiquitination[1, 4, 5, 6, 7, 8, 10]
1230AASGYPVKVPLEVQEacetylation[12]
1230AASGYPVKVPLEVQEubiquitination[1, 2]
1242VQEADEAKLQQTEAEubiquitination[1, 2, 9]
1262EAIALFQKML*****ubiquitination[1, 2, 5, 6, 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] 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]
 [3] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] 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]
 [6] 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]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [11] 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]
 [12] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1264 AA 
Protein Sequence
MSTLYVSPHP DAFPSLRALI AARYGEAGEG PGWGGAHPRI CLQPPPTSRT SFPPPRLPAL 60
EQGPGGLWVW GATAVAQLLW PAGLGGPGGS RAAVLVQQWV SYADTELIPA ACGATLPALG 120
LRSSAQDPQA VLGALGRALS PLEEWLRLHT YLAGEAPTLA DLAAVTALLL PFRYVLDPPA 180
RRIWNNVTRW FVTCVRQPEF RAVLGEVVLY SGARPLSHQP GPEAPALPKT AAQLKKEAKK 240
REKLEKFQQK QKIQQQQPPP GEKKPKPEKR EKRDPGVITY DLPTPPGEKK DVSGPMPDSY 300
SPRYVEAAWY PWWEQQGFFK PEYGRPNVSA ANPRGVFMMC IPPPNVTGSL HLGHALTNAI 360
QDSLTRWHRM RGETTLWNPG CDHAGIATQV VVEKKLWREQ GLSRHQLGRE AFLQEVWKWK 420
EEKGDRIYHQ LKKLGSSLDW DRACFTMDPK LSAAVTEAFV RLHEEGIIYR STRLVNWSCT 480
LNSAISDIEV DKKELTGRTL LSVPGYKEKV EFGVLVSFAY KVQGSDSDEE VVVATTRIET 540
MLGDVAVAVH PKDTRYQHLK GKNVIHPFLS RSLPIVFDEF VDMDFGTGAV KITPAHDQND 600
YEVGQRHGLE AISIMDSRGA LINVPPPFLG LPRFEARKAV LVALKERGLF RGIEDNPMVV 660
PLCNRSKDVV EPLLRPQWYV RCGEMAQAAS AAVTRGDLRI LPEAHQRTWH AWMDNIREWC 720
ISRQLWWGHR IPAYFVTVSD PAVPPGEDPD GRYWVSGRNE AEAREKAAKE FGVSPDKISL 780
QQDEDVLDTW FSSGLFPLSI LGWPNQSEDL SVFYPGTLLE TGHDILFFWV ARMVMLGLKL 840
TGRLPFREVY LHAIVRDAHG RKMSKSLGNV IDPLDVIYGI SLQGLHNQLL NSNLDPSEVE 900
KAKEGQKADF PAGIPECGTD ALRFGLCAYM SQGRDINLDV NRILGYRHFC NKLWNATKFA 960
LRGLGKGFVP SPTSQPGGHE SLVDRWIRSR LTEAVRLSNQ GFQAYDFPAV TTAQYSFWLY 1020
ELCDVYLECL KPVLNGVDQV AAECARQTLY TCLDVGLRLL SPFMPFVTEE LFQRLPRRMP 1080
QAPPSLCVTP YPEPSECSWK DPEAEAALEL ALSITRAVRS LRADYNLTRI RPDCFLEVAD 1140
EATGALASAV SGYVQALASA GVVAVLALGA PAPQGCAVAL ASDRCSIHLQ LQGLVDPARE 1200
LGKLQAKRVE AQRQAQRLRE RRAASGYPVK VPLEVQEADE AKLQQTEAEL RKVDEAIALF 1260
QKML 1264 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:InterPro.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0004832; F:valine-tRNA ligase activity; IEA:InterPro.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC.
 GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR010987; Glutathione-S-Trfase_C-like.
 IPR004045; Glutathione_S-Trfase_N.
 IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
 IPR004046; GST_C.
 IPR014729; Rossmann-like_a/b/a_fold.
 IPR009080; tRNAsynth_1a_anticodon-bd.
 IPR013155; V/L/I-tRNA-synth_anticodon-bd.
 IPR009008; Val/Leu/Ile-tRNA-synth_edit.
 IPR002303; Valyl-tRNA_ligase. 
Pfam
 PF08264; Anticodon_1
 PF00043; GST_C
 PF02798; GST_N
 PF00133; tRNA-synt_1 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I
 PS50405; GST_CTER 
PRINTS
 PR00986; TRNASYNTHVAL.