CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044431
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isoleucine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Isoleucine-tRNA synthetase, isoform CRA_d 
Gene Name
 IARS 
Gene Synonyms/Alias
 hCG_31137 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22MRYSAEWKSTVSRLGubiquitination[1]
158ARLSALYKLESDYEIubiquitination[2, 3]
175RFPGAYLKGKKYRPLubiquitination[1, 4]
188PLFDYFLKCKENGAFubiquitination[4]
234MDFNIIRKDSLPVCPubiquitination[4]
261DFAGQYVKDADKSIIubiquitination[2, 4]
265QYVKDADKSIIRTLKacetylation[5]
265QYVKDADKSIIRTLKubiquitination[4]
300SDTPLIYKAVPSWFVubiquitination[1, 3, 4, 6, 7]
340KRFGNWLKDARDWTIubiquitination[2, 4, 8]
435VHYPFENKREFEDAFubiquitination[7]
507DPVSIIQKYGADALRubiquitination[2, 3, 4]
531RAENLRFKEEGVRDVubiquitination[4]
562QNVLRLQKEEEIEFLubiquitination[1, 2, 4]
706VREELIDKKTESAVSubiquitination[4]
707REELIDKKTESAVSQubiquitination[4]
734DRKTIPIKYPLKEIVubiquitination[4]
738IPIKYPLKEIVVIHQubiquitination[2]
751HQDPEALKDIKSLEKacetylation[5]
751HQDPEALKDIKSLEKubiquitination[4]
754PEALKDIKSLEKYIIubiquitination[4]
758KDIKSLEKYIIEELNubiquitination[1, 4, 6]
775KVTLSTDKNKYGIRLubiquitination[4]
777TLSTDKNKYGIRLRAubiquitination[4]
793PDHMVLGKRLKGAFKubiquitination[4]
800KRLKGAFKAVMTSIKubiquitination[4]
807KAVMTSIKQLSSEELacetylation[5]
807KAVMTSIKQLSSEELubiquitination[2, 3, 4, 6]
819EELEQFQKTGTIVVEubiquitination[2, 4, 9]
889NRIQKLRKKCNLVPTubiquitination[4]
904DEITVYYKAKSEGTYubiquitination[4]
932TTIKAPLKPYPVSPSubiquitination[1, 2, 3, 4]
941YPVSPSDKVLIQEKTacetylation[1]
941YPVSPSDKVLIQEKTubiquitination[1, 2, 3, 4, 6]
947DKVLIQEKTQLKGSEacetylation[5]
947DKVLIQEKTQLKGSEubiquitination[1, 2, 4]
951IQEKTQLKGSELEITubiquitination[1, 2, 3, 4]
1003DNRLDLLKLKSVVTSubiquitination[4]
1005RLDLLKLKSVVTSIFubiquitination[1, 2, 4]
1134ITEDIPVKTLNMKTVubiquitination[1, 2, 3, 4]
1139PVKTLNMKTVYVSVLubiquitination[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Aminoacyl-tRNA synthetase; Complete proteome; Ligase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1152 AA 
Protein Sequence
MGITEYNNQC RAIVMRYSAE WKSTVSRLGR WIDFDNDYKT LYPQFMESVW WVFKQLYDKG 60
LVYRGVKVMP FSTACNTPLS NFESHQNYKD VQDPSVFVTF PLEEDETVSL VAWTTTPWTL 120
PSNLAVCVNP EMQYVKIKDV ARGRLLILME ARLSALYKLE SDYEILERFP GAYLKGKKYR 180
PLFDYFLKCK ENGAFTVLVD NYVKEEEGTG VVHQAPYFGA EDYRVCMDFN IIRKDSLPVC 240
PVDASGCFTT EVTDFAGQYV KDADKSIIRT LKEQGRLLVA TTFTHSYPFC WRSDTPLIYK 300
AVPSWFVRVE NMVDQLLRNN DLCYWVPELV REKRFGNWLK DARDWTISRN RYWGTPIPLW 360
VSDDFEEVVC IGSVAELEEL SGAKISDLHR ESVDHLTIPS RCGKGSLHRI SEVFDCWFES 420
GSMPYAQVHY PFENKREFED AFPADFIAEG IDQTRGWFYT LLVLATALFG QPPFKNVIVN 480
GLVLASDGQK MSKRKKNYPD PVSIIQKYGA DALRLYLINS PVVRAENLRF KEEGVRDVLK 540
DVLLPWYNAY RFLIQNVLRL QKEEEIEFLY NENTVRESPN ITDRWILSFM QSLIGFFETE 600
MAAYRLYTVV PRLVKFVDIL TNWYVRMNRR RLKGENGMED CVMALETLFS VLLSLCRLMA 660
PYTPFLTELM YQNLKVLIDP VSVQDKDTLS IHYLMLPRVR EELIDKKTES AVSQMQSVIE 720
LGRVIRDRKT IPIKYPLKEI VVIHQDPEAL KDIKSLEKYI IEELNVRKVT LSTDKNKYGI 780
RLRAEPDHMV LGKRLKGAFK AVMTSIKQLS SEELEQFQKT GTIVVEGHEL HDEDIRLMYT 840
FDQATGGTAQ FEAHSDAQAL VLLDVTPDQS MVDEGMAREV INRIQKLRKK CNLVPTDEIT 900
VYYKAKSEGT YLNSVIESHT EFIFTTIKAP LKPYPVSPSD KVLIQEKTQL KGSELEITLT 960
RGSSLPGPAC AYVNLNICAN GSEQGGVLLL ENPKGDNRLD LLKLKSVVTS IFGVKNTELA 1020
VFHDETEIQN QTDLLSLSGK TLCVTAGSAP SLINSSSTLL CQYINLQLLN AKPQECLMGT 1080
VGTLLLENPL GQNGLTHQGL LYEAAKVFGL RSRKLKLFLN ETQTQEITED IPVKTLNMKT 1140
VYVSVLPTTA DF 1152 
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:0004822; F:isoleucine-tRNA ligase activity; IEA:InterPro.
 GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:InterPro.
 GO:0006450; P:regulation of translational fidelity; IEA:GOC. 
Interpro
 IPR002300; aa-tRNA-synth_Ia.
 IPR002301; Ile-tRNA-ligase.
 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
  
PRINTS
 PR00984; TRNASYNTHILE.