CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020781
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial 
Protein Synonyms/Alias
 2-oxoglutarate dehydrogenase complex component E2; OGDC-E2; Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2K 
Gene Name
 Dlst 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
153KTGAAPAKAKPAETPacetylation[1]
155GAAPAKAKPAETPAPacetylation[1, 2, 3, 4]
155GAAPAKAKPAETPAPsuccinylation[3]
268QEMRARHKDAFLKKHacetylation[1, 2, 4, 5, 6, 7]
273RHKDAFLKKHNLKLGacetylation[1, 2, 4, 5, 6, 7]
274HKDAFLKKHNLKLGFacetylation[1]
278FLKKHNLKLGFMSAFacetylation[1, 2, 4, 5, 8]
308AVIDDATKEVVYRDYacetylation[1, 6, 7]
354TINELGEKARKNELAacetylation[1, 2, 3, 4]
354TINELGEKARKNELAsuccinylation[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [6] 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]
 [7] 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]
 [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] 
Functional Description
 The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). 
Sequence Annotation
 DOMAIN 72 144 Lipoyl-binding.
 ACT_SITE 425 425 Potential.
 ACT_SITE 429 429 Potential.
 MOD_RES 111 111 N6-lipoyllysine (Potential).  
Keyword
 Acyltransferase; Alternative splicing; Complete proteome; Direct protein sequencing; Lipoyl; Mitochondrion; Reference proteome; Transferase; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 454 AA 
Protein Sequence
MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCRGP GYPDNRKMVI NSGSVFRVRF 60
FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE DEVVCEIETD KTSVQVPSPA 120
NGIIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAETP APAHKAEPAA PAAPPPPAAP 180
VLTQMPPVPS PSQPPSSKPV SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK 240
EAQNTCAMLT TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN 300
AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE LGEKARKNEL 360
AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHAI FDRPVAVGGK VEVRPMMYVA 420
LTYDHRLIDG REAVTFLRKI KAAVEDPRVL LLDL 454 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
 GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:EC.
 GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
 GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 
Interpro
 IPR003016; 2-oxoA_DH_lipoyl-BS.
 IPR001078; 2-oxoacid_DH_actylTfrase.
 IPR000089; Biotin_lipoyl.
 IPR023213; CAT-like_dom.
 IPR011053; Single_hybrid_motif.
 IPR006255; SucB. 
Pfam
 PF00198; 2-oxoacid_dh
 PF00364; Biotin_lipoyl 
SMART
  
PROSITE
 PS50968; BIOTINYL_LIPOYL
 PS00189; LIPOYL 
PRINTS