CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007482
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isoleucine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Isoleucyl-tRNA synthetase; IRS; IleRS 
Gene Name
 IARS 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
98PVEYEIDKTLGIRGPubiquitination[1]
110RGPEDVAKMGITEYNubiquitination[1, 2]
169VFKQLYDKGLVYRGVubiquitination[3]
268ARLSALYKLESDYEIubiquitination[3, 4]
285RFPGAYLKGKKYRPLubiquitination[1]
298PLFDYFLKCKENGAFubiquitination[1]
344MDFNIIRKDSLPVCPubiquitination[1]
371DFAGQYVKDADKSIIubiquitination[1, 3]
375QYVKDADKSIIRTLKubiquitination[1]
410SDTPLIYKAVPSWFVubiquitination[1, 3, 4, 5, 6]
450KRFGNWLKDARDWTIubiquitination[1, 3, 7]
617DPVSIIQKYGADALRubiquitination[1, 3, 4]
641RAENLRFKEEGVRDVubiquitination[1]
672QNVLRLQKEEEIEFLubiquitination[1, 3]
816VREELIDKKTESAVSubiquitination[1]
817REELIDKKTESAVSQubiquitination[1]
844DRKTIPIKYPLKEIVacetylation[8]
844DRKTIPIKYPLKEIVubiquitination[1]
848IPIKYPLKEIVVIHQubiquitination[3]
861HQDPEALKDIKSLEKubiquitination[1]
864PEALKDIKSLEKYIIubiquitination[1]
868KDIKSLEKYIIEELNubiquitination[1, 5, 6]
885KVTLSTDKNKYGIRLubiquitination[1]
887TLSTDKNKYGIRLRAubiquitination[1]
903PDHMVLGKRLKGAFKubiquitination[1]
910KRLKGAFKAVMTSIKubiquitination[1]
917KAVMTSIKQLSSEELubiquitination[1, 3, 4, 5, 6]
929EELEQFQKTGTIVVEubiquitination[1, 3]
999NRIQKLRKKCNLVPTubiquitination[1]
1000RIQKLRKKCNLVPTDubiquitination[1]
1014DEITVYYKAKSEGTYubiquitination[1]
1042TTIKAPLKPYPVSPSubiquitination[1, 3, 4]
1051YPVSPSDKVLIQEKTubiquitination[1, 3, 4, 5, 6]
1057DKVLIQEKTQLKGSEubiquitination[1, 3]
1061IQEKTQLKGSELEITubiquitination[1, 3, 4]
1113DNRLDLLKLKSVVTSubiquitination[1, 3]
1115RLDLLKLKSVVTSIFubiquitination[1, 3]
1244ITEDIPVKTLNMKTVubiquitination[1, 3, 4]
1249PVKTLNMKTVYVSVLubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
  
Sequence Annotation
 MOTIF 48 58 "HIGH" region.
 MOTIF 600 604 "KMSKS" region.
 BINDING 603 603 ATP (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 1047 1047 Phosphoserine.
 MOD_RES 1049 1049 Phosphoserine.  
Keyword
 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
 1262 AA 
Protein Sequence
MLQQVPENIN FPAEEEKILE FWTEFNCFQE CLKQSKHKPK FTFYDGPPFA TGLPHYGHIL 60
AGTIKDIVTR YAHQSGFHVD RRFGWDCHGL PVEYEIDKTL GIRGPEDVAK MGITEYNNQC 120
RAIVMRYSAE WKSTVSRLGR WIDFDNDYKT LYPQFMESVW WVFKQLYDKG LVYRGVKVMP 180
FSTACNTPLS NFESHQNYKD VQDPSVFVTF PLEEDETVSL VAWTTTPWTL PSNLAVCVNP 240
EMQYVKIKDV ARGRLLILME ARLSALYKLE SDYEILERFP GAYLKGKKYR PLFDYFLKCK 300
ENGAFTVLVD NYVKEEEGTG VVHQAPYFGA EDYRVCMDFN IIRKDSLPVC PVDASGCFTT 360
EVTDFAGQYV KDADKSIIRT LKEQGRLLVA TTFTHSYPFC WRSDTPLIYK AVPSWFVRVE 420
NMVDQLLRNN DLCYWVPELV REKRFGNWLK DARDWTISRN RYWGTPIPLW VSDDFEEVVC 480
IGSVAELEEL SGAKISDLHR ESVDHLTIPS RCGKGSLHRI SEVFDCWFES GSMPYAQVHY 540
PFENKREFED AFPADFIAEG IDQTRGWFYT LLVLATALFG QPPFKNVIVN GLVLASDGQK 600
MSKRKKNYPD PVSIIQKYGA DALRLYLINS PVVRAENLRF KEEGVRDVLK DVLLPWYNAY 660
RFLIQNVLRL QKEEEIEFLY NENTVRESPN ITDRWILSFM QSLIGFFETE MAAYRLYTVV 720
PRLVKFVDIL TNWYVRMNRR RLKGENGMED CVMALETLFS VLLSLCRLMA PYTPFLTELM 780
YQNLKVLIDP VSVQDKDTLS IHYLMLPRVR EELIDKKTES AVSQMQSVIE LGRVIRDRKT 840
IPIKYPLKEI VVIHQDPEAL KDIKSLEKYI IEELNVRKVT LSTDKNKYGI RLRAEPDHMV 900
LGKRLKGAFK AVMTSIKQLS SEELEQFQKT GTIVVEGHEL HDEDIRLMYT FDQATGGTAQ 960
FEAHSDAQAL VLLDVTPDQS MVDEGMAREV INRIQKLRKK CNLVPTDEIT VYYKAKSEGT 1020
YLNSVIESHT EFIFTTIKAP LKPYPVSPSD KVLIQEKTQL KGSELEITLT RGSSLPGPAC 1080
AYVNLNICAN GSEQGGVLLL ENPKGDNRLD LLKLKSVVTS IFGVKNTELA VFHDETEIQN 1140
QTDLLSLSGK TLCVTAGSAP SLINSSSTLL CQYINLQLLN AKPQECLMGT VGTLLLENPL 1200
GQNGLTHQGL LYEAAKVFGL RSRKLKLFLN ETQTQEITED IPVKTLNMKT VYVSVLPTTA 1260
DF 1262 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004822; F:isoleucine-tRNA ligase activity; TAS:Reactome.
 GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC.
 GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. 
Interpro
 IPR001412; aa-tRNA-synth_I_CS.
 IPR002300; aa-tRNA-synth_Ia.
 IPR002301; Ile-tRNA-ligase.
 IPR023586; Ile-tRNA-ligase_type2.
 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. 
Pfam
 PF08264; Anticodon_1
 PF00133; tRNA-synt_1 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00984; TRNASYNTHILE.