CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014230
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2-oxoglutarate dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 2-oxoglutarate dehydrogenase complex component E1; OGDC-E1; Alpha-ketoglutarate dehydrogenase 
Gene Name
 Ogdh 
Gene Synonyms/Alias
 Kiaa4192 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
237QCQWIRQKFETPGIMacetylation[1]
401YCGDTEGKKVMSILLacetylation[1, 2]
534YKQIRKQKPVLQKYAacetylation[1]
561EYEEEISKYDKICEEacetylation[3]
564EEISKYDKICEEAFTacetylation[4]
564EEISKYDKICEEAFTsuccinylation[4]
619DVLFHIGKVASSVPVacetylation[5]
697LHDQNVDKRTCIPMNacetylation[1]
897PAAQDPHKVKRLLFCacetylation[1, 6]
899AQDPHKVKRLLFCTGacetylation[6]
947LLLKEAQKYPNAELAacetylation[1]
970QGYYDYVKPRLRTTIacetylation[1, 3, 4]
970QGYYDYVKPRLRTTIsuccinylation[4]
999AAPATGNKKTHLTELacetylation[2]
1020AFDLDAFKKFS****ubiquitination[7]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] 
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 three enzymatic components: 2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). 
Sequence Annotation
 REGION 933 939 Recognized by alloreactive CD8 cytotoxic
 MOD_RES 970 970 N6-acetyllysine (By similarity).
 CROSSLNK 534 534 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Glycolysis; Isopeptide bond; Mitochondrion; Oxidoreductase; Reference proteome; Thiamine pyrophosphate; Transit peptide; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1023 AA 
Protein Sequence
MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE 60
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV 120
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES 180
DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET 240
PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN 300
GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR 360
VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV 420
YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP 480
EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY 540
AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR 600
SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA 660
FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL 720
SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP 780
HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH 840
VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR 900
LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH 960
KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK 1020
KFS 1023 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
 GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Compara.
 GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IDA:MGI.
 GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
 GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
 GO:0006103; P:2-oxoglutarate metabolic process; IEA:Compara.
 GO:0021695; P:cerebellar cortex development; IEP:UniProtKB.
 GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
 GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
 GO:0021766; P:hippocampus development; IEP:UniProtKB.
 GO:0006734; P:NADH metabolic process; IEA:Compara.
 GO:0061034; P:olfactory bulb mitral cell layer development; IEP:UniProtKB.
 GO:0021860; P:pyramidal neuron development; IEP:UniProtKB.
 GO:0021756; P:striatum development; IEP:UniProtKB.
 GO:0006104; P:succinyl-CoA metabolic process; IEA:Compara.
 GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEP:UniProtKB.
 GO:0021794; P:thalamus development; IEP:UniProtKB.
 GO:0006099; P:tricarboxylic acid cycle; IEA:Compara. 
Interpro
 IPR011603; 2oxoglutarate_DH_E1.
 IPR001017; DH_E1.
 IPR005475; Transketolase-like_Pyr-bd. 
Pfam
 PF00676; E1_dh
 PF02779; Transket_pyr 
SMART
 SM00861; Transket_pyr 
PROSITE
  
PRINTS