CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040168
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
117KKARSFAKAAIEKQKacetylation[1]
150FDGKYEAKQLRTFYQacetylation[1]
161TFYQMYDKGLVYRSYacetylation[2]
169GLVYRSYKPVFWSPSacetylation[1, 2, 3]
169GLVYRSYKPVFWSPSubiquitination[4]
205YVKFPLLKPSPKLASacetylation[2]
373EGTDVVIKMLQTAKNubiquitination[4]
386KNLLKEEKLVHSYPYacetylation[2]
386KNLLKEEKLVHSYPYubiquitination[4]
468PVFHHKTKDEYLINSacetylation[2]
468PVFHHKTKDEYLINSubiquitination[5]
589HGFTLGEKGEKMSKSubiquitination[6]
615NGGQDQSKEPPYGADubiquitination[5, 7, 8]
709YKQYDFGKVVRLLRTacetylation[1, 2]
731NFYFSIIKDRLYCEKacetylation[2]
800STSSIWKKPGLEEAVubiquitination[6]
824FLGSIPGKNAAEYKVubiquitination[5, 6]
887DVIELKGKFLINLEGubiquitination[6]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 940 AA 
Protein Sequence
MKLLGRQQPD TELEIQQKCG FSELYSWQRE RKVKTEFCLH DGPPYANGDP HVGHALNKIL 60
KDIANRFHMM NGSKIHFVPG WDCHGLPIEI KVLSELGREA QNLSAMEIRK KARSFAKAAI 120
EKQKSAFIRW GIMADWNNCY YTFDGKYEAK QLRTFYQMYD KGLVYRSYKP VFWSPSSRTA 180
LAEAELEYNP EHVSRSIYVK FPLLKPSPKL ASLIDGSSPV SILVWTTQPW TIPANEAVCY 240
MPESKYAVVK CSKSGDLYVL AADKVASVAS TLETTFETIS TLSGVDLENG TCSHPLIPDK 300
ASPLLPANHV TMAKGTGLVH TAPAHGMEDY GVASQHNLPM DCLVDEDGVF TDVAGPELQN 360
KAVLEEGTDV VIKMLQTAKN LLKEEKLVHS YPYDWRTKKP VVIRASKQWF INITDIKTAA 420
KELLKKVKFI PGSALNGMVE MMDRRPYWCI SRQRVWGVPI PVFHHKTKDE YLINSQTTEH 480
IVKLVEQHGS DIWWTLPPEQ LLPKEVLSEV GGPDALEYVP GQDILDIWFD SGTSWSYVLP 540
GPDQRADLYL EGKDQLGGWF QSSLLTSVAA RKRAPYKTVI VHGFTLGEKG EKMSKSLGNV 600
IHPDVVVNGG QDQSKEPPYG ADVLRWWVAD SNVFTEVAIG PSVLNAARDD ISKLRNTLRF 660
LLGNVADFNP ETDSIPVNDM YVIDQYMLHL LQDLANKITE LYKQYDFGKV VRLLRTFYTR 720
ELSNFYFSII KDRLYCEKEN DPKRRSCQTA LVEILDVIVR SFAPILPHLA EEVFQHIPYI 780
KEPKSVFRTG WISTSSIWKK PGLEEAVESA CAMRDSFLGS IPGKNAAEYK VITVIEPGLL 840
FEIIEMLQSE ETSSTSQLNE LMMASESTLL AQEPREMTAD VIELKGKFLI NLEGGDIREE 900
SSYKVIVMPT TKEKCPRCWK YTAESSDTLC PRCAEVVSGK 940 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 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
 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.