CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038151
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Isoleucine--tRNA ligase, mitochondrial 
Protein Synonyms/Alias
  
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
56DSPQSSSKGGRYRDTacetylation[1]
56DSPQSSSKGGRYRDTsuccinylation[1]
74PQTSFPMKLLGRQQSacetylation[1, 2, 3, 4, 5, 6]
74PQTSFPMKLLGRQQSsuccinylation[1]
194FAQAAIEKQKSAFVRacetylation[1, 6]
194FAQAAIEKQKSAFVRsuccinylation[1]
222FDPKYEAKQLRVFYQacetylation[6]
233VFYQMYEKGLVYRSYubiquitination[7]
241GLVYRSYKPVYWSPSacetylation[1, 3, 4, 6, 8]
241GLVYRSYKPVYWSPSsuccinylation[1]
479PVLIRASKQWFVNITacetylation[1]
479PVLIRASKQWFVNITsuccinylation[1]
497AAAKESLKTVKFIPGacetylation[9]
500KESLKTVKFIPGAALacetylation[1, 3, 5, 6]
500KESLKTVKFIPGAALsuccinylation[1]
540PVFHHKTKDEYLINSacetylation[5, 6, 9]
667EKGEKMSKSLGNVINacetylation[1]
667EKGEKMSKSLGNVINsuccinylation[1]
683DTIISGGKDHSKEPPacetylation[1]
683DTIISGGKDHSKEPPsuccinylation[1]
687SGGKDHSKEPPYGADacetylation[1]
687SGGKDHSKEPPYGADsuccinylation[1]
Reference
 [1] 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]
 [2] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 733 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
DDISKVRPAQ GTL 733 
Gene Ontology
 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:InterPro.
 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.
 IPR009008; Val/Leu/Ile-tRNA-synth_edit. 
Pfam
 PF00133; tRNA-synt_1 
SMART
  
PROSITE
 PS00178; AA_TRNA_LIGASE_I 
PRINTS
 PR00984; TRNASYNTHILE.