CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016473
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
74PQTSFPMKLLGRQQSacetylation[1]
106WQRERKVKTEFCLHDacetylation[1]
194FAQAAIEKQKSAFVRacetylation[1]
222FDPKYEAKQLRVFYQacetylation[1]
233VFYQMYEKGLVYRSYacetylation[1]
233VFYQMYEKGLVYRSYubiquitination[2]
241GLVYRSYKPVYWSPSacetylation[1]
479PVLIRASKQWFVNITacetylation[1]
497AAAKESLKTVKFIPGacetylation[1]
500KESLKTVKFIPGAALacetylation[1]
540PVFHHKTKDEYLINSacetylation[1]
661HGFTLGEKGEKMSKSacetylation[1]
725AARDDISKLRNTLRFacetylation[1, 3, 4, 5]
775TKITDSYKQYDFGKVacetylation[1, 4, 5, 6, 7, 8, 9]
775TKITDSYKQYDFGKVsuccinylation[9]
781YKQYDFGKVVRLLKAacetylation[3, 9]
781YKQYDFGKVVRLLKAsuccinylation[9]
787GKVVRLLKAFYTRELacetylation[3]
803SFYFSIVKDRLYCENacetylation[3, 4, 5, 6]
856IPYVTEPKSVFRTGWacetylation[3]
Reference
 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [4] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [7] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [8] 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]
 [9] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
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 233 233 N6-acetyllysine (By similarity).
 MOD_RES 241 241 N6-acetyllysine (By similarity).
 MOD_RES 775 775 N6-acetyllysine (By similarity).
 MOD_RES 781 781 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Mitochondrion; Nucleotide-binding; Protein biosynthesis; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1012 AA 
Protein Sequence
MHWGLCPRGP GAAAVAAAGS FWGPARLPSR LGCLGMTRRL VVRSVAGADS PQSSSKGGRY 60
RDTVLLPQTS FPMKLLGRQQ SDMELEIQQK CGFSELYSWQ RERKVKTEFC LHDGPPYANG 120
DPHVGHALNK ILKDIANRFH MMRGSKVHFV PGWDCHGLPI ETKVLSELGV DAQSLSAMEI 180
REKARSFAQA AIEKQKSAFV RWGVMADWNN CYYTFDPKYE AKQLRVFYQM YEKGLVYRSY 240
KPVYWSPSSR TALAEAELEY NPEHVSRSIY VRFPLLRPPP KLESLTDASS PVSVLVWTTQ 300
PWTIPANQAI CYMPEAKYAV VKCSASGHLY ILAEDKIAPV ASALETTFDV VAAFSGVDLE 360
GGTCSHPLTP DKVSPLLPAT HVTMAKGTGL VHTAPAHGME DYSVASQHSL PMDCLVDEGG 420
MFTDAAGPEL QNKAVLKEGT DVVIKMLQAT KNVLKEENIV HSYPCDWRTK TPVLIRASKQ 480
WFVNITDIKA AAKESLKTVK FIPGAALNSM TDMLDRRPYW CISRQRVWGV PIPVFHHKTK 540
DEYLINSQTT EHIIKLVEQH GSDVWWTLPA EQLLPAEVLA QAGGPGALEY APGQDILDIW 600
FDSGTSWSCV LQDTQQRADL YLEGKDQLGG WFQSSLLTSV ATRSKAPFRT VMVHGFTLGE 660
KGEKMSKSLG NVINPDTIIS GGKDHSKEPP YGADILRWWI AESNVFTEVT IGPSVLSAAR 720
DDISKLRNTL RFLLGNLTGF NPETDSVPVK NMYVIDQYML HLIQDFATKI TDSYKQYDFG 780
KVVRLLKAFY TRELSSFYFS IVKDRLYCEN EKDPKRRSCQ TALAEILDVL VRAFAPILPH 840
LAEEVFQHIP YVTEPKSVFR TGWINTSSIW KKPGLEEAVE SACAMRDSFL GSIPGKNAAE 900
YEVIIVIEPG LLFEIMEMLQ AEETSSTSQL NELMMASQTT LLAQEPRERT AGDIELTGTF 960
VINLEGGDIR EESSYKVIVV PTAREKCPRC WKHTSETADA LCPRCAEVIG AK 1012 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 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. 
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.