CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022122
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isoleucine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
 Isoleucyl-tRNA synthetase; IleRS 
Gene Name
 IARS2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
189KKARSFAKAAIEKQKacetylation[1]
233TFYQMYDKGLVYRSYacetylation[1]
241GLVYRSYKPVFWSPSacetylation[1]
241GLVYRSYKPVFWSPSubiquitination[2, 3]
445EGTDVVIKMLQTAKNubiquitination[2, 3]
458KNLLKEEKLVHSYPYubiquitination[2, 3]
540PVFHHKTKDEYLINSubiquitination[4]
661HGFTLGEKGEKMSKSacetylation[1]
661HGFTLGEKGEKMSKSubiquitination[5]
687NGGQDQSKEPPYGADubiquitination[4, 6]
775NKITELYKQYDFGKVacetylation[1]
781YKQYDFGKVVRLLRTacetylation[1]
803NFYFSIIKDRLYCEKacetylation[7]
872STSSIWKKPGLEEAVubiquitination[5]
896FLGSIPGKNAAEYKVubiquitination[4, 5]
959DVIELKGKFLINLEGubiquitination[5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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] 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]
 [7] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
  
Sequence Annotation
 MOTIF 116 126 "HIGH" region (By similarity).
 MOTIF 664 668 "KMSKS" region (By similarity).
 BINDING 667 667 ATP (By similarity).
 MOD_RES 189 189 N6-acetyllysine.
 MOD_RES 233 233 N6-acetyllysine.
 MOD_RES 241 241 N6-acetyllysine.
 MOD_RES 775 775 N6-acetyllysine.
 MOD_RES 781 781 N6-acetyllysine.  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Polymorphism; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1012 AA 
Protein Sequence
MRWGLRPRGP GAAALATARS LWGTPRLPCS PGWQGATKRL LVRSVSGASN HQPNSNSGRY 60
RDTVLLPQTS FPMKLLGRQQ PDTELEIQQK CGFSELYSWQ RERKVKTEFC LHDGPPYANG 120
DPHVGHALNK ILKDIANRFH MMNGSKIHFV PGWDCHGLPI EIKVLSELGR EAQNLSAMEI 180
RKKARSFAKA AIEKQKSAFI RWGIMADWNN CYYTFDGKYE AKQLRTFYQM YDKGLVYRSY 240
KPVFWSPSSR TALAEAELEY NPEHVSRSIY VKFPLLKPSP KLASLIDGSS PVSILVWTTQ 300
PWTIPANEAV CYMPESKYAV VKCSKSGDLY VLAADKVASV ASTLETTFET ISTLSGVDLE 360
NGTCSHPLIP DKASPLLPAN HVTMAKGTGL VHTAPAHGME DYGVASQHNL PMDCLVDEDG 420
VFTDVAGPEL QNKAVLEEGT DVVIKMLQTA KNLLKEEKLV HSYPYDWRTK KPVVIRASKQ 480
WFINITDIKT AAKELLKKVK FIPGSALNGM VEMMDRRPYW CISRQRVWGV PIPVFHHKTK 540
DEYLINSQTT EHIVKLVEQH GSDIWWTLPP EQLLPKEVLS EVGGPDALEY VPGQDILDIW 600
FDSGTSWSYV LPGPDQRADL YLEGKDQLGG WFQSSLLTSV AARKRAPYKT VIVHGFTLGE 660
KGEKMSKSLG NVIHPDVVVN GGQDQSKEPP YGADVLRWWV ADSNVFTEVA IGPSVLNAAR 720
DDISKLRNTL RFLLGNVADF NPETDSIPVN DMYVIDQYML HLLQDLANKI TELYKQYDFG 780
KVVRLLRTFY TRELSNFYFS IIKDRLYCEK ENDPKRRSCQ TALVEILDVI VRSFAPILPH 840
LAEEVFQHIP YIKEPKSVFR TGWISTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE 900
YKVITVIEPG LLFEIIEMLQ SEETSSTSQL NELMMASEST LLAQEPREMT ADVIELKGKF 960
LINLEGGDIR EESSYKVIVM PTTKEKCPRC WKYTAESSDT LCPRCAEVVS GK 1012 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004822; F:isoleucine-tRNA ligase activity; IEA:EC.
 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.
 IPR023585; Ile-tRNA-ligase_type1.
 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.
 IPR010663; Znf_DNA_glyclase/IsotRNA_synth. 
Pfam
 PF08264; Anticodon_1
 PF00133; tRNA-synt_1
 PF06827; zf-FPG_IleRS 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00984; TRNASYNTHILE.